# Coiled coil

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Structural motif in proteins

For other uses, see [Coiled coil (disambiguation)](/source/Coiled_coil_(disambiguation)).

Figure 1: The classic example of a coiled coil is the GCN4 [leucine zipper](/source/Leucine_zipper) (PDB accession code 1zik), which is a parallel, left-handed [homodimer](/source/Homodimer). However, many other types of coiled coil exist.

A **coiled coil** is a [structural motif](/source/Structural_motif) in [proteins](/source/Protein) in which two to seven[1] [alpha-helices](/source/Alpha_helix) are coiled together like the strands of a rope. ([Dimers](/source/Protein_dimer) and [trimers](/source/Protein_trimer) are the most common types.) They have been found in roughly 5-10% of proteins and have a variety of functions.[2] They are one of the most widespread motifs found in protein-protein interactions. To aid protein study, several tools have been developed to predict coiled-coils in protein structures.[3] Many coiled coil-type proteins are involved in important biological functions, such as the regulation of [gene expression](/source/Gene_expression) — e.g., [transcription factors](/source/Transcription_factor). Notable examples are the [oncoproteins](/source/Oncoprotein) [c-Fos](/source/C-Fos) and [c-Jun](/source/C-Jun), as well as the muscle protein [tropomyosin](/source/Tropomyosin).

## Discovery

The possibility of coiled coils for α-[keratin](/source/Keratin) was initially somewhat controversial. [Linus Pauling](/source/Linus_Pauling) and [Francis Crick](/source/Francis_Crick) independently came to the conclusion that this was possible at about the same time. In the summer of 1952, Pauling visited the laboratory in [England](/source/England) where Crick worked. Pauling and Crick met and spoke about various topics; at one point, Crick asked whether Pauling had considered *coiled coils* (a term Crick came up with), to which Pauling said he had. Upon returning to the United States, Pauling resumed research on the topic. He concluded that coiled coils exist, and submitted a lengthy manuscript to the journal *[Nature](/source/Nature_(journal))* in October. Pauling's son Peter Pauling worked at the same lab as Crick, and mentioned the report to him. Crick believed that Pauling had stolen his idea, and submitted a shorter note to *Nature* a few days after Pauling's manuscript arrived. Eventually, after some controversy and frequent correspondences, Crick's lab declared that the idea had been reached independently by both researchers, and that no intellectual theft had occurred.[4] In his note (which was published first due to its shorter length), Crick proposed the *coiled coil* and as well as mathematical methods for determining their structure.[5] Remarkably, this was soon after the structure of the [alpha helix](/source/Alpha_helix) was suggested in 1951 by [Linus Pauling](/source/Linus_Pauling) and coworkers.[6] These studies were published in the absence of knowledge of a keratin sequence. The first keratin sequences were determined by Hanukoglu and Fuchs in 1982.[7][8]

Based on sequence and secondary structure prediction analyses identified the coiled-coil domains of keratins.[8] These models have been confirmed by structural analyses of coiled-coil domains of keratins.[9]

## Molecular structure

Coiled coils usually contain a repeated pattern, *hxxhcxc*, of hydrophobic (*h*) and charged (*c*) [amino-acid](/source/Amino-acid) residues, referred to as a [heptad repeat](/source/Heptad_repeat).[10] The positions in the heptad repeat are usually labeled *abcdefg*, where *a* and *d* are the hydrophobic positions, often being occupied by [isoleucine](/source/Isoleucine), [leucine](/source/Leucine), or [valine](/source/Valine). Folding a sequence with this repeating pattern into an [alpha-helical](/source/Alpha-helix) [secondary structure](/source/Secondary_structure) causes the hydrophobic residues to be presented as a 'stripe' that coils gently around the helix in left-handed fashion, forming an [amphipathic](/source/Amphiphile) structure. The most favorable way for two such helices to arrange themselves in the water-filled environment of the [cytoplasm](/source/Cytoplasm) is to wrap the hydrophobic strands against each other sandwiched between the [hydrophilic](/source/Hydrophilic) amino acids. Thus, it is the burial of hydrophobic surfaces that provides the [thermodynamic](/source/Thermodynamic) driving force for the oligomerization. The packing in a coiled-coil interface is exceptionally tight, with almost complete [van der Waals](/source/Van_der_Waals_force) contact between the [side-chains](/source/Substituent) of the *a* and *d* residues. This tight packing was originally predicted by [Francis Crick](/source/Francis_Crick) in 1952[5] and is referred to as [knobs into holes packing](/source/Knobs_into_holes_packing).

The [α-helices](/source/Alpha-helix) may be parallel or anti-parallel, and usually adopt a *left-handed* super-coil (Figure 1). Although disfavored, a few *right-handed* coiled coils have also been observed in nature and in designed proteins.[11]

## Biological roles

As coiled-coil domains are common among a significant amount of proteins in a wide variety of protein families, they help proteins fulfill various functions in the cell. Their primary feature is to facilitate protein-protein interaction and keep proteins or domains interlocked. This feature corresponds to several subfunctions, including membrane fusion, molecular spacing, oligomerization tags, vesicle movement, aid in movement proteins, cell structure, and more.[12]

### Membrane fusion

Side view of the gp41 hexamer that initiates the entry of HIV into its target cell.

A coiled coil domain plays a role in [human immunodeficiency virus type 1](/source/Human_immunodeficiency_virus_type_1) (HIV-1) infection. Viral entry into CD4-positive cells commences when three subunits of a glycoprotein 120 ([gp120](/source/Gp120)) bind to CD4 receptor and a coreceptor.[13] Glycoprotein gp120 is closely associated with a trimer of [gp41](/source/Gp41) via van der Waals interactions. Eventually, the gp41 N-terminal fusion peptide sequence anchors into the host cell. A [spring-loaded](/source/Spring-loaded) mechanism is responsible for bringing the viral and cell membranes in close enough proximity that they will fuse. The origin of the spring-loaded mechanism lies within the exposed gp41, which contains two consecutive heptad repeats (HR1 and HR2) following the fusion peptide at the N terminus of the protein. HR1 forms a parallel, trimeric coiled coil onto which HR2 region coils, forming the trimer-of-hairpins (or six-helix bundle) structure, thereby facilitating membrane fusion through bringing the membranes close to each other.[14] The virus then enters the cell and begins its replication. Recently, inhibitors derived from HR2 such as [Fuzeon](/source/Enfuvirtide) (DP178, T-20) that bind to the HR1 region on gp41 have been developed.[15] However, peptides derived from HR1 have little viral inhibition efficacy due to the propensity for these peptides to aggregate in solution. Chimeras of these HR1-derived peptides with GCN4 [leucine zippers](/source/Leucine_zipper) have been developed and have shown to be more active than [Fuzeon](/source/Enfuvirtide).[16] [Human immunodeficiency virus type 2](/source/Human_immunodeficiency_virus_type_2) has a membrane envelope glycoprotein with similar structure to HIV-1 gp41, but containing substitutions for a glycine amino acid residue in the coiled coil domain that may impact trimer stability.[17]

The proteins [SNAP-25](/source/SNAP25), [synaptobrevin](/source/Synaptobrevin), and [syntaxin-1](/source/STX1A) have alpha-helices which interact with each other to form a coiled-coil [SNARE complex](/source/SNARE_protein). Zippering the domains together provides the necessary energy for vesicle fusion to occur.[18]

### Molecular spacers

The coiled-coil motif may also act as a spacer between two objects within a cell. The lengths of these molecular spacer coiled-coil domains are highly conserved. The purpose of these molecular spacers may be to separate protein domains, thus keeping them from interacting, or to separate vesicles within the cell to mediate vesicle transport. An example of this first purpose is Omp‐α found in *[T. maritima](/source/Thermotoga_maritima)*.[19] Other proteins keep vesicles apart, such as p115, [giantin](/source/Giantin), and [GM130](/source/GM130) which interact with each other via coiled-coil motifs and act as a tether between the [Golgi](/source/Golgi_apparatus) and a nearby vesicle.[20] The family of proteins related to this activity of tethering vesicles to the Golgi are known as golgins.[21] Finally, there are several proteins with coiled-coil domains involved in the [kinetochore](/source/Kinetochore), which keeps [chromosomes](/source/Chromosome) separated during [cell division](/source/Cell_division). These proteins include [Ndc-80](/source/NDC80), and [Nuf2p](/source/NUF2). Related proteins interact with [microtubules](/source/Microtubule) during cell division, of which mutation leads to cell death.[22]

### As oligomerization tags

Because of their specific interaction coiled coils can be used as "tags" to stabilize or enforce a specific oligomerization state.[23] A coiled coil interaction has been observed to drive the oligomerization of the [BBS2](/source/BBS2) and [BBS7](/source/BBS7) subunits of the [BBSome](/source/BBSome).[24][25] Because coiled-coils generally interact with other coiled coils, they are found in proteins which are required to form dimers or tetramers with more copies of themselves.[26] Because of their ability in driving [protein oligomerization](/source/Protein_oligomer), they have also been studied in their use in forming synthetic nanostructures.[27]

## Design

Secondary and tertiary structure of the coiled-coil motif. The heptad repeat often consists of specific amino acids, seen in the figure. Knobs into holes packing is also shown.[28]

The general problem of deciding on the folded structure of a protein when given the amino acid sequence (the so-called [protein folding problem](/source/Protein_structure_prediction)) has only been solved partially. However, the coiled coil is one of a relatively small number of folding motifs for which the relationships between the sequence and the final folded structure are comparatively well understood.[29][30] Harbury *et al.* performed a landmark study using an archetypal coiled coil, GCN4, in which rules that govern the way that peptide sequence affects the oligomeric state (that is, the number of [alpha-helices](/source/Alpha-helix) in the final assembly) were established.[31][32] The GCN4 coiled coil is a 31-amino-acid (which equates to just over four *heptads*) parallel, dimeric (i.e., consisting of two [alpha-helices](/source/Alpha-helix)) coiled coil and has a repeated [isoleucine](/source/Isoleucine) (or I, in [single-letter code](/source/Amino_acid#Table_of_standard_amino_acid_abbreviations_and_properties)) and [leucine](/source/Leucine) (L) at the *a* and *d* positions, respectively, and forms a dimeric coiled coil. When the amino acids in the *a* and *d* positions were changed from I at *a* and L at *d* to I at *a* and I at *d*, a trimeric (three alpha-helices) coiled coil was formed. Furthermore, switching the positions of L to *a* and I to *d* resulted in the formation of a tetrameric (four [alpha-helices](/source/Alpha-helix)) coiled coil. These represent a set of rules for the determination of coiled coil oligomeric states and allows scientists to effectively "dial-in" the oligomerization behavior. Another aspect of coiled coil assembly that is relatively well understood, at least in the case of dimeric coiled coils, is that placing a polar residue (in particular [asparagine](/source/Asparagine), N) at opposing *a* positions forces parallel assembly of the coiled coil. This effect is due to a self-complementary [hydrogen bonding](/source/Hydrogen_bond) between these residues, which would go unsatisfied if an N were paired with, for instance, an L on the opposing helix.[33]

It was recently demonstrated by Peacock, [Pikramenou](/source/Zoe_Pikramenou) and co-workers that coiled coils may be self-assembled using lanthanide(III) ions as a template, thus producing novel imaging agents.[34]

## Biomedical applications

Some examples of protein nanostructures made using coiled-coil motifs. The top three pictures shown in the figure more accurately models the nanostructure, while the pictures underneath describe their basic shape. These may be used as building blocks to create further nanostructures.[28]

Coiled-coil motifs have been experimented on as possible building block for [nanostructures](/source/Nanostructure), in part because of their simple design and wide range of function based primarily on facilitating protein-protein interaction. Simple guidelines for [de novo synthesis](/source/De_novo_synthesis) of new proteins containing coiled-coil domains have led to many applications being hypothesized, including drug delivery, regenerating tissue, protein origami, and much more.[35] In regards to drug delivery, coiled-coil domains would help overcome some of the hazards of chemotherapeutic drugs, by keeping them from leaking into healthy tissue as they are transported to their target. Coiled-coil domains can be made to bind to specific proteins or cell surface markers, allowing for more precise targeting in drug delivery.[36] Other functions would be to help store and transport drugs within the body that would otherwise degrade rapidly, by creating nanotubes and other structure svia the interlocking of coiled-coil motifs.[35] By utilizing the function of oligomerization of proteins via coiled-coil domains, antigen display can be amplified in vaccines, increasing their effectiveness.[37]

The oligomerization of coiled-coil motifs allows for the creation of protein origami and protein building blocks. Metal-ligand interactions, covalent bonds, and ionic interactions have been studied to manipulate possible coiled-coil interactions in this field of study.[35] Several different nanostructures can be made by combining coiled-coil motifs such that they are self-assembling building blocks. However, several difficulties remain with stability.[38] Using peptides with coiled-coil motifs for scaffolding has made it easier to create 3D structures for cell culturing. 3D hydrogels can be made with these peptides, and then cells may be loaded into the matrix.[39] This has applications in the study of tissue, tissue engineering, and more.[35]

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1. **[^](#cite_ref-Harbury1993_31-0)** Harbury PB, Zhang T, Kim PS, Alber T (November 1993). "A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants". *Science*. **262** (5138): 1401–1407. [Bibcode](/source/Bibcode_(identifier)):[1993Sci...262.1401H](https://ui.adsabs.harvard.edu/abs/1993Sci...262.1401H). [doi](/source/Doi_(identifier)):[10.1126/science.8248779](https://doi.org/10.1126%2Fscience.8248779). [PMID](/source/PMID_(identifier)) [8248779](https://pubmed.ncbi.nlm.nih.gov/8248779). [S2CID](/source/S2CID_(identifier)) [45833675](https://api.semanticscholar.org/CorpusID:45833675).

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1. **[^](#cite_ref-34)** Berwick MR, Lewis DJ, Jones AW, Parslow RA, [Dafforn TR](/source/Tim_Dafforn), Cooper HJ, et al. (January 2014). ["De novo design of Ln(III) coiled coils for imaging applications"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3950886). *Journal of the American Chemical Society*. **136** (4): 1166–1169. [doi](/source/Doi_(identifier)):[10.1021/ja408741h](https://doi.org/10.1021%2Fja408741h). [PMC](/source/PMC_(identifier)) [3950886](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3950886). [PMID](/source/PMID_(identifier)) [24405157](https://pubmed.ncbi.nlm.nih.gov/24405157).

1. ^ [***a***](#cite_ref-Jorgensen-2022_35-0) [***b***](#cite_ref-Jorgensen-2022_35-1) [***c***](#cite_ref-Jorgensen-2022_35-2) [***d***](#cite_ref-Jorgensen-2022_35-3) Jorgensen, Michael D.; Chmielewski, Jean (2022). "Recent advances in coiled-coil peptide materials and their biomedical applications". *Chemical Communications*. **58** (83): 11625–11636. [doi](/source/Doi_(identifier)):[10.1039/d2cc04434j](https://doi.org/10.1039%2Fd2cc04434j). [ISSN](/source/ISSN_(identifier)) [1359-7345](https://search.worldcat.org/issn/1359-7345). [PMID](/source/PMID_(identifier)) [36172799](https://pubmed.ncbi.nlm.nih.gov/36172799). [S2CID](/source/S2CID_(identifier)) [252514360](https://api.semanticscholar.org/CorpusID:252514360).

1. **[^](#cite_ref-36)** McFarlane, Ainsley A.; Orriss, George L.; Stetefeld, Jörg (December 2009). ["The use of coiled-coil proteins in drug delivery systems"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094320). *European Journal of Pharmacology*. **625** (1–3): 101–107. [doi](/source/Doi_(identifier)):[10.1016/j.ejphar.2009.05.034](https://doi.org/10.1016%2Fj.ejphar.2009.05.034). [PMC](/source/PMC_(identifier)) [7094320](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094320). [PMID](/source/PMID_(identifier)) [19835864](https://pubmed.ncbi.nlm.nih.gov/19835864).

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## Further reading

- Crick FH (1953). ["The Packing of α-Helices: Simple Coiled-Coils"](https://doi.org/10.1107%2FS0365110X53001964). *Acta Crystallogr*. **6** (8): 689–697. [Bibcode](/source/Bibcode_(identifier)):[1953AcCry...6..689C](https://ui.adsabs.harvard.edu/abs/1953AcCry...6..689C). [doi](/source/Doi_(identifier)):[10.1107/S0365110X53001964](https://doi.org/10.1107%2FS0365110X53001964).

- Nishikawa K, Scheraga HA (1976). "Geometrical criteria for formation of coiled-coil structures of polypeptide chains". *Macromolecules*. **9** (3): 395–407. [Bibcode](/source/Bibcode_(identifier)):[1976MaMol...9..395N](https://ui.adsabs.harvard.edu/abs/1976MaMol...9..395N). [doi](/source/Doi_(identifier)):[10.1021/ma60051a004](https://doi.org/10.1021%2Fma60051a004). [PMID](/source/PMID_(identifier)) [940353](https://pubmed.ncbi.nlm.nih.gov/940353).

- Harbury PB, Zhang T, Kim PS, Alber T (November 1993). "A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants". *Science*. **262** (5138): 1401–1407. [Bibcode](/source/Bibcode_(identifier)):[1993Sci...262.1401H](https://ui.adsabs.harvard.edu/abs/1993Sci...262.1401H). [doi](/source/Doi_(identifier)):[10.1126/science.8248779](https://doi.org/10.1126%2Fscience.8248779). [PMID](/source/PMID_(identifier)) [8248779](https://pubmed.ncbi.nlm.nih.gov/8248779). [S2CID](/source/S2CID_(identifier)) [45833675](https://api.semanticscholar.org/CorpusID:45833675).

- Gonzalez L, Plecs JJ, Alber T (June 1996). "An engineered allosteric switch in leucine-zipper oligomerization". *Nature Structural Biology*. **3** (6): 510–515. [doi](/source/Doi_(identifier)):[10.1038/nsb0696-510](https://doi.org/10.1038%2Fnsb0696-510). [PMID](/source/PMID_(identifier)) [8646536](https://pubmed.ncbi.nlm.nih.gov/8646536). [S2CID](/source/S2CID_(identifier)) [30381026](https://api.semanticscholar.org/CorpusID:30381026).

- Harbury PB, Plecs JJ, Tidor B, Alber T, Kim PS (November 1998). "High-resolution protein design with backbone freedom". *Science*. **282** (5393): 1462–1467. [doi](/source/Doi_(identifier)):[10.1126/science.282.5393.1462](https://doi.org/10.1126%2Fscience.282.5393.1462). [PMID](/source/PMID_(identifier)) [9822371](https://pubmed.ncbi.nlm.nih.gov/9822371).

- Yu YB (October 2002). "Coiled-coils: stability, specificity, and drug delivery potential". *Advanced Drug Delivery Reviews*. **54** (8): 1113–1129. [doi](/source/Doi_(identifier)):[10.1016/S0169-409X(02)00058-3](https://doi.org/10.1016%2FS0169-409X%2802%2900058-3). [PMID](/source/PMID_(identifier)) [12384310](https://pubmed.ncbi.nlm.nih.gov/12384310).

- Burkhard P, Ivaninskii S, Lustig A (May 2002). "Improving coiled-coil stability by optimizing ionic interactions". *Journal of Molecular Biology*. **318** (3): 901–910. [doi](/source/Doi_(identifier)):[10.1016/S0022-2836(02)00114-6](https://doi.org/10.1016%2FS0022-2836%2802%2900114-6). [PMID](/source/PMID_(identifier)) [12054832](https://pubmed.ncbi.nlm.nih.gov/12054832).

- Gillingham AK, Munro S (August 2003). ["Long coiled-coil proteins and membrane traffic"](https://doi.org/10.1016%2FS0167-4889%2803%2900088-0). *Biochimica et Biophysica Acta (BBA) - Molecular Cell Research*. **1641** (2–3): 71–85. [doi](/source/Doi_(identifier)):[10.1016/S0167-4889(03)00088-0](https://doi.org/10.1016%2FS0167-4889%2803%2900088-0). [PMID](/source/PMID_(identifier)) [12914949](https://pubmed.ncbi.nlm.nih.gov/12914949).

- Mason JM, Arndt KM (February 2004). "Coiled coil domains: stability, specificity, and biological implications". *ChemBioChem*. **5** (2): 170–176. [doi](/source/Doi_(identifier)):[10.1002/cbic.200300781](https://doi.org/10.1002%2Fcbic.200300781). [PMID](/source/PMID_(identifier)) [14760737](https://pubmed.ncbi.nlm.nih.gov/14760737). [S2CID](/source/S2CID_(identifier)) [39252601](https://api.semanticscholar.org/CorpusID:39252601).

## External links

- [Coiled-coil domains of keratins](http://www.proteopedia.org/wiki/index.php/Keratins)

### Coiled-coil related software

#### Prediction, detection, and visualization

- [Deprecated link](https://en.wikipedia.org/wiki/Wikipedia:Archive.today_guidance) at [archive.today](/source/Archive.today) (archived 2012-12-23)

- [Deprecated link](https://en.wikipedia.org/wiki/Wikipedia:Archive.today_guidance) at [archive.today](/source/Archive.today) (archived 2002-01-11)

- [Paircoil2](http://groups.csail.mit.edu/cb/paircoil2) / [Paircoil](http://groups.csail.mit.edu/cb/paircoil)

- [bCIPA](http://www.syntbio.net/bCIPA/) Estimates Tm values for coiled coil pairs

- [bCIPA library screen](https://people.bath.ac.uk/jm2219/biology/bcipa-library.php) Screens a library of sequences against a single defined target and estimates Tm values for all coiled coils pairs.

- [bCIPA Interactome Screen](http://people.bath.ac.uk/jm2219/biology/bcipa-interactome.php) Screens all interactions between a selection of defined sequences and estimates Tm values for all coiled coil pairs.

- [STRAP](http://3d-alignment.eu/) contains an algorithm to predict coiled-coils from AA-sequences.

- [PrOCoil](http://www.bioinf.jku.at/software/procoil/) predicts the oligomerization of coiled coil proteins and visualizes the contribution of each individual amino acid to the overall oligomeric tendency.

- [DrawCoil](http://www.grigoryanlab.org/drawcoil/) creates helical wheel diagrams for coiled coils of any oligomerization state and orientation.

#### Databases

- [Spiricoil](http://supfam.org/SUPERFAMILY/spiricoil) uses protein domain annotation to predict coiled coil presence and oligormeric state for all completely sequenced organisms

- [CC+](http://coiledcoils.chm.bris.ac.uk/ccplus/search/) [Archived](https://web.archive.org/web/20111108092907/http://coiledcoils.chm.bris.ac.uk/ccplus/search/) 2011-11-08 at the [Wayback Machine](/source/Wayback_Machine) is a [relational database](/source/Relational_database) of coiled coils found in the [PDB](/source/Protein_data_bank)

- [SUPERFAMILY](http://supfam.org/SUPERFAMILY) protein domain annotation for all completely sequenced organisms based on the expertly curated [SCOP](/source/Structural_Classification_of_Proteins) coiled coil class

v t e Protein tandem repeats Fibrous: Coiled coil Collagen helix Elongated: Alpha solenoid Ankyrin repeat Armadillo repeat Transcription activator-like effector Beta solenoid Beta helix Antifreeze protein HEAT repeat Leucine-rich repeat Pentapeptide repeat Tetratricopeptide repeat Trefoil knot fold Closed: Beta barrel Beta trefoil fold Beta-propeller Kelch motif TIM barrel WD40 repeat Beads-on-a-string: Sushi domain See also: Repeated sequence (DNA)

v t e Protein secondary structure Protein secondary structure Helices: α-helix 310 helix π-helix β-helix Polyproline helix Collagen helix Extended: β-strand Turn Beta turn Beta hairpin Beta bulge α-strand Supersecondary: Coiled coil Helix-turn-helix

---
Adapted from the Wikipedia article [Coiled coil](https://en.wikipedia.org/wiki/Coiled_coil) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Coiled_coil?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.