β sandwich

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β-sandwich structure made of Tenascin C ( 1st TEN )

A β-sandwich is a protein domain with at least two opposing (anti-parallel) β-strands and at least one β-loop .

properties

β-sandwich domains are divided into different classes according to their protein folding . The β-sandwich of immunoglobulins consists of seven to nine antiparallel strands in two β-sheets . The jelly roll fold occurs in some carbohydrate- binding proteins such as the lectin Concanavalin A , in the collagen- binding domain of the adhesive of Staphylococcus aureus and in the fibronectin- binding domains of Tenascin . The type L lectin domain is a variant of the jelly roll fold. The C2 domain in protein kinase C -C2 has an eight-strand β sandwich.

literature

  • DN Woolfson, PA Evans, EG Hutchinson, JM Thornton: Topological and stereochemical restrictions in beta-sandwich protein structures. In: Protein engineering. Volume 6, Number 5, July 1993, pp. 461-470, ISSN  0269-2139 . PMID 8415573 .

Individual evidence

  1. ↑ AE Kister, AS Fokas, TS Papatheodorou, IM Gelfand: Strict rules determine arrangements of strands in sandwich proteins . In: PNAS . 103, No. 11, 2006, pp. 4107-4110. doi : 10.1073 / pnas.0510747103 . PMID 16537492 .