# Fibrillin

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Protein family

Not to be confused with [Fibrin](/source/Fibrin).

fibrillin 1 Crystallographic structure of the cbEGF9-hybrid2-cbEGF10 region of human fibrillin 1.[1] Identifiers Symbol FBN1 Alt. symbols FBN, MFS1, WMS NCBI gene 2200 HGNC 3603 OMIM 134797 PDB 2W86 RefSeq NM_000138 UniProt P35555 Other data Locus Chr. 15 q21.1 Search for Structures Swiss-model Domains InterPro

fibrillin 2 Identifiers Symbol FBN2 Alt. symbols CCA NCBI gene 2201 HGNC 3604 OMIM 121050 RefSeq NM_001999 UniProt P35556 Other data Locus Chr. 5 q23-q31 Search for Structures Swiss-model Domains InterPro

fibrillin 3 Identifiers Symbol FBN3 NCBI gene 84467 HGNC 18794 OMIM 608529 RefSeq NM_032447 UniProt Q75N90 Other data Locus Chr. 19 p13 Search for Structures Swiss-model Domains InterPro

**Fibrillin** is a [glycoprotein](/source/Glycoprotein), which is essential for the formation of [elastic fibers](/source/Elastic_fiber) found in [connective tissue](/source/Connective_tissue).[2] Fibrillin is secreted into the [extracellular matrix](/source/Extracellular_matrix) by [fibroblasts](/source/Fibroblasts) and becomes incorporated into the insoluble [microfibrils](/source/Microfibril), which appear to provide a scaffold for deposition of [elastin](/source/Elastin).[3]

## Clinical aspects

[Marfan syndrome](/source/Marfan_syndrome) is a genetic disorder of the connective tissue caused by defected [FBN1](/source/FBN1) gene. Mutations in [FBN1](/source/FBN1) and [FBN2](/source/FBN2) are also sometimes associated with [adolescent idiopathic scoliosis](/source/Adolescent_idiopathic_scoliosis).[4]

## Types

### Fibrillin-1

[Fibrillin-1](/source/FBN1) is a major component of the [microfibrils](/source/Microfibril) that form a sheath surrounding the amorphous [elastin](/source/Elastin). It is believed that the [microfibrils](/source/Microfibril) are composed of end-to-end [polymers](/source/Polymer) of fibrillin. To date, 3 forms of fibrillin have been described. The fibrillin-1 protein was isolated by Engvall in 1986,[5] and mutations in the FBN1 gene cause [Marfan syndrome](/source/Marfan_syndrome).[6][7]

This protein is found in humans, and its gene is found on chromosome 15. At present more than 1500 different mutations have been described.[1][7]

#### Structure

There is no complete, high-resolution structure of fibrillin-1. Instead, short fragments have been produced recombinantly and their structures solved by X-ray crystallography or using NMR spectroscopy. A recent example is the structure of the fibrillin-1 hybrid2 domain, in context of its flanking calcium binding epidermal growth factor domains, which was determined using X-ray crystallography to a resolution of 1.8 Å.[1] The microfibrils that are made up of fibrillin protein are responsible for different cell-matrix interactions in the human body.

### Fibrillin-2

Fibrillin-2 was isolated in 1994 by Zhang[8] and is thought to play a role in early [elastogenesis](/source/Elastogenesis). Mutations in the fibrillin-2 gene have been linked to [Beals syndrome](/source/Beals_syndrome).

### Fibrillin-3

More recently, fibrillin-3 was described and is believed to be located mainly in the brain.[9] Along with the brain, fibrillin-3 has been localized in the gonads and ovaries of field mice.

### Fibrillin-4

Fibrillin-4 was first discovered in zebrafish, and has a sequence similar to fibrillin-2.[10]

## References

1. ^ [***a***](#cite_ref-pmid19446531_1-0) [***b***](#cite_ref-pmid19446531_1-1) [***c***](#cite_ref-pmid19446531_1-2) [PDB](/source/Protein_Data_Bank): [2W86](https://www.rcsb.org/structure/2W86)​; Jensen SA, Iqbal S, Lowe ED, Redfield C, Handford PA (May 2009). ["Structure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteins"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2724076). *Structure*. **17** (5): 759–68. [doi](/source/Doi_(identifier)):[10.1016/j.str.2009.03.014](https://doi.org/10.1016%2Fj.str.2009.03.014). [PMC](/source/PMC_(identifier)) [2724076](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2724076). [PMID](/source/PMID_(identifier)) [19446531](https://pubmed.ncbi.nlm.nih.gov/19446531).

1. **[^](#cite_ref-pmid11911778_2-0)** Kielty CM, Baldock C, Lee D, Rock MJ, Ashworth JL, Shuttleworth CA (February 2002). ["Fibrillin: from microfibril assembly to biomechanical function"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1692929). *Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences*. **357** (1418): 207–17. [doi](/source/Doi_(identifier)):[10.1098/rstb.2001.1029](https://doi.org/10.1098%2Frstb.2001.1029). [PMC](/source/PMC_(identifier)) [1692929](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1692929). [PMID](/source/PMID_(identifier)) [11911778](https://pubmed.ncbi.nlm.nih.gov/11911778).

1. **[^](#cite_ref-Singh2006_3-0)** Singh (2006). [*Textbook of human histology*](https://books.google.com/books?id=Ej22iANgNkoC&pg=PA64). Jaypee Brothers Publishers. pp. 64–. [ISBN](/source/ISBN_(identifier)) [978-81-8061-809-3](https://en.wikipedia.org/wiki/Special:BookSources/978-81-8061-809-3). Retrieved 9 December 2010.[*[permanent dead link](https://en.wikipedia.org/wiki/Wikipedia:Link_rot)*]

1. **[^](#cite_ref-4)** Buchan JG, Alvarado DM, Haller GE, Cruchaga C, Harms MB, Zhang T, Willing MC, Grange DK, Braverman AC, Miller NH, Morcuende JA, Tang NL, Lam TP, Ng BK, Cheng JC, Dobbs MB, [Gurnett CA](/source/Christina_Gurnett) (October 2014). ["Rare variants in FBN1 and FBN2 are associated with severe adolescent idiopathic scoliosis"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4159151). *Human Molecular Genetics*. **23** (19): 5271–82. [doi](/source/Doi_(identifier)):[10.1093/hmg/ddu224](https://doi.org/10.1093%2Fhmg%2Fddu224). [PMC](/source/PMC_(identifier)) [4159151](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4159151). [PMID](/source/PMID_(identifier)) [24833718](https://pubmed.ncbi.nlm.nih.gov/24833718).

1. **[^](#cite_ref-pmid3536967_5-0)** Sakai LY, Keene DR, Engvall E (December 1986). ["Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114568). *The Journal of Cell Biology*. **103** (6 Pt 1): 2499–509. [doi](/source/Doi_(identifier)):[10.1083/jcb.103.6.2499](https://doi.org/10.1083%2Fjcb.103.6.2499). [PMC](/source/PMC_(identifier)) [2114568](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114568). [PMID](/source/PMID_(identifier)) [3536967](https://pubmed.ncbi.nlm.nih.gov/3536967).

1. **[^](#cite_ref-pmid20818846_6-0)** Dietz HC (August 2010). ["New therapeutic approaches to mendelian disorders"](https://doi.org/10.1056%2FNEJMra0907180). *The New England Journal of Medicine*. **363** (9): 852–63. [doi](/source/Doi_(identifier)):[10.1056/NEJMra0907180](https://doi.org/10.1056%2FNEJMra0907180). [PMID](/source/PMID_(identifier)) [20818846](https://pubmed.ncbi.nlm.nih.gov/20818846).

1. ^ [***a***](#cite_ref-pmid26124674_7-0) [***b***](#cite_ref-pmid26124674_7-1) von Kodolitsch Y, De Backer J, Schüler H, Bannas P, Behzadi C, Bernhardt AM, Hillebrand M, Fuisting B, Sheikhzadeh S, Rybczynski M, Kölbel T, Püschel K, Blankenberg S, Robinson PN (2015). ["Perspectives on the revised Ghent criteria for the diagnosis of Marfan syndrome"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4476478). *The Application of Clinical Genetics*. **8**: 137–55. [doi](/source/Doi_(identifier)):[10.2147/TACG.S60472](https://doi.org/10.2147%2FTACG.S60472). [PMC](/source/PMC_(identifier)) [4476478](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4476478). [PMID](/source/PMID_(identifier)) [26124674](https://pubmed.ncbi.nlm.nih.gov/26124674).

1. **[^](#cite_ref-8)** Zhang H, Apfelroth SD, Hu W, Davis EC, Sanguineti C, Bonadio J, Mecham RP, Ramirez F (March 1994). ["Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119952). *The Journal of Cell Biology*. **124** (5): 855–63. [doi](/source/Doi_(identifier)):[10.1083/jcb.124.5.855](https://doi.org/10.1083%2Fjcb.124.5.855). [PMC](/source/PMC_(identifier)) [2119952](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2119952). [PMID](/source/PMID_(identifier)) [8120105](https://pubmed.ncbi.nlm.nih.gov/8120105).

1. **[^](#cite_ref-pmid14962672_9-0)** Corson GM, Charbonneau NL, Keene DR, Sakai LY (March 2004). "Differential expression of fibrillin-3 adds to microfibril variety in human and avian, but not rodent, connective tissues". *Genomics*. **83** (3): 461–72. [doi](/source/Doi_(identifier)):[10.1016/j.ygeno.2003.08.023](https://doi.org/10.1016%2Fj.ygeno.2003.08.023). [PMID](/source/PMID_(identifier)) [14962672](https://pubmed.ncbi.nlm.nih.gov/14962672).

1. **[^](#cite_ref-pmid18816837_10-0)** Gansner JM, Madsen EC, Mecham RP, Gitlin JD (October 2008). ["Essential role for fibrillin-2 in zebrafish notochord and vascular morphogenesis"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3081706). *Developmental Dynamics*. **237** (10): 2844–61. [doi](/source/Doi_(identifier)):[10.1002/dvdy.21705](https://doi.org/10.1002%2Fdvdy.21705). [PMC](/source/PMC_(identifier)) [3081706](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3081706). [PMID](/source/PMID_(identifier)) [18816837](https://pubmed.ncbi.nlm.nih.gov/18816837).

## External links

- [Fibrillin](https://meshb.nlm.nih.gov/record/ui?name=Fibrillin) at the U.S. National Library of Medicine [Medical Subject Headings](/source/Medical_Subject_Headings) (MeSH)

v t e Connective tissue Physiology Soft tissue Fibrosis Scarring Composition Cells Resident Fibroblast Fibrocyte Reticular cell Tendon cell Adipocyte Melanocyte Wandering cells Mast cell Macrophage Extracellular matrix Ground substance Tissue fluid Fibers Collagen fibers Reticular fibers COL3A1 Elastic fibers Elastin Fibrillin FBN1 FBN2 FBN3 EMILIN1 Elaunin Types Proper Loose Reticular Adipose Brown White Dense Dense irregular connective tissue Submucosa Dermis Dense regular connective tissue Ligament Tendon Aponeurosis Embryonic Mucoid Mesenchymal Specialized Cartilage Elastic Hyaline Fibrocartilage Bone Blood

v t e Proteins of the cytoskeleton Human Microfilaments and ABPs Myofilament Actins A1 A2 B C1 G1 G2 Myosins I MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B LC MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1 Other Tropomodulin 1 2 3 4 Troponin T 1 2 3 C 1 2 I 1 2 3 Tropomyosin 1 2 3 4 Actinin 1 2 3 4 Arp2/3 complex actin depolymerizing factors Cofilin 1 2 Destrin Gelsolin Profilin 1 2 Titin Other Wiskott–Aldrich syndrome protein Fibrillin Filamin FLNA FLNB FLNC Espin TRIOBP Intermediate filaments Type 1/2 (Keratin, Cytokeratin) Epithelial keratins (soft alpha-keratins) type I/chromosome 17 9 10 12 13 14 15 16 17 19 20 chromosome 12 18 none 21 type II/chromosome 12 1 2A 3 4 5 6A 6B 6C 7 8 Hair keratins (hard alpha-keratins) type I/chromosome 17 31 32 33A 33B 34 35 36 37 38 type II/chromosome 12 81 82 83 84 85 86 Ungrouped alpha chromosome 17 23 24 25 26 27 28 39 40 chromosome 12 71 72 73 74 75 76 77 78 79 80 Not alpha Beta-keratin Type 3 Desmin GFAP Peripherin Vimentin Type 4 Internexin Nestin Neurofilament NEFL NEFM NEFH Synemin Syncoilin Type 5 Nuclear lamins A/C B1 B2 Microtubules and MAPs Tubulins TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 TUBB TUBB1 TUBB2A TUBB2B TUBB2C TUBB3 TUBB4A TUBB4Q TUBB6 TUBB8 TUBG1 TUBG2 TUBGCP2 TUBGCP3 TUBGCP4 TUBGCP5 TUBGCP6 TUBD1 TUBE1 MAPs EB1 EB2 EB3 MAP1A MAP1B MAP2 MAP4 Kinesins KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3 Dyneins axonemal: DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 cytoplasmic: DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3 Microtubule organising proteins CAMSAP1 CAMSAP2 CAMSAP3 Centrin 1 Centrin 2 Centrin 3 PCM1 Microtubule severing proteins Katanin Spastin Other Tau protein Dynactin DCTN1 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3 Catenins Alpha catenin Beta catenin APC Plakoglobin (gamma catenin) Delta catenin GAN Membrane Dystrophin Dystroglycan Utrophin Ankyrin ANK1 ANK2 ANK3 Spectrin SPTA1 SPTAN1 SPTB SPTBN1 SPTBN2 SPTBN4 SPTBN5 Other Plakins Corneodesmosin Desmoplakin Dystonin Envoplakin MACF1 Periplakin Plectin Talin TLN1 Vinculin Plakophilin PKP1 PKP2 ACF7 PLEKHA7 Nonhuman Major sperm proteins Prokaryotic cytoskeleton Crescentin FtsZ MreB ParM See also: cytoskeletal defects

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