# Beta-sandwich

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Two opposing antiparallel beta sheets that commonly occur in proteins

Illustration of the β-sandwich from [Tenascin C](/source/Tenascin_C) (PDB entry: [1TEN](https://www.rcsb.org/structure/1TEN)​).

**Beta-sandwich** or **β-sandwich** domains consisting of 80 to 350 amino acids occur commonly in [proteins](/source/Protein). They are characterized by two opposing antiparallel [beta sheets](/source/Beta_sheet) (β-sheets).[1] The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds. The [immunoglobulin-type fold](/source/Immunoglobulin_domain) found in [antibodies](/source/Antibodies) (Ig-fold) consists of a sandwich arrangement of 7-9 antiparallel [β-strands](/source/%CE%92-strand) arranged in two [β-sheets](/source/Beta_sheet) with a [Greek-key topology](/source/Beta_sheet#Greek_key_motif).[2] The Greek-key topology is also found in [Human](/source/Human) [Transthyretin](/source/Transthyretin). The [jelly-roll](/source/Jelly_roll_fold) topology is found in carbohydrate binding proteins such as [concanavalin A](/source/Concanavalin_A) and various [lectins](/source/Lectins), in the [collagen](/source/Collagen) binding domain of *[Staphylococcus aureus](/source/Staphylococcus_aureus)* [Adhesin](/source/Bacterial_adhesin) and in modules that bind [fibronectin](/source/Fibronectin) as found in [Tenascin](/source/Tenascin) (Third Fibronectin Type III Repeat). The [L-type lectin domain](/source/L-type_lectin_domain) is a variation of the jelly roll fold. The [C2 domain](/source/C2_domain) in its typical version (PKC-C2) is a β-sandwich composed of 8 [beta-strands](/source/Beta-strand) (β-strands).

## References

1. **[^](#cite_ref-Kister_1-0)** Kister, A. E.; Fokas, A. S.; Papatheodorou, T. S.; Gelfand, I. M. (2006). ["Strict rules determine arrangements of strands in sandwich proteins"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1449654). *PNAS*. **103** (11): 4107–4110. [Bibcode](/source/Bibcode_(identifier)):[2006PNAS..103.4107K](https://ui.adsabs.harvard.edu/abs/2006PNAS..103.4107K). [doi](/source/Doi_(identifier)):[10.1073/pnas.0510747103](https://doi.org/10.1073%2Fpnas.0510747103). [PMC](/source/PMC_(identifier)) [1449654](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1449654). [PMID](/source/PMID_(identifier)) [16537492](https://pubmed.ncbi.nlm.nih.gov/16537492).

1. **[^](#cite_ref-2)** Bokhove, Marcel; Jovine, Luca (2018-01-01), Litscher, Eveline S.; [Wassarman, Paul M.](/source/Paul_M_Wassarman) (eds.), ["Chapter Thirteen - Structure of Zona Pellucida Module Proteins"](http://www.sciencedirect.com/science/article/pii/S0070215318300395), *Current Topics in Developmental Biology*, Extracellular Matrix and Egg Coats, **130**, Academic Press: 413–442, [doi](/source/Doi_(identifier)):[10.1016/bs.ctdb.2018.02.007](https://doi.org/10.1016%2Fbs.ctdb.2018.02.007), [PMID](/source/PMID_(identifier)) [29853186](https://pubmed.ncbi.nlm.nih.gov/29853186), retrieved 2020-12-15

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