| 词条 | Beta-sandwich |
| 释义 |
β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel 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 found in antibodies (Ig-fold) consists of a sandwich arrangement of 7 and 9 antiparallel β-strands arranged in two β-sheets with a Greek-key topology. The Greek-key topology is also found in Human Transthyretin. The jelly-roll topology is found in carbohydrate binding proteins such as concanavalin A and various lectins, in the collagen binding domain of Staphylococcus aureus Adhesin and in modules that bind fibronectin as found in Tenascin (Third Fibronectin Type III Repeat). The L-type lectin domain is a variation of the jelly roll fold. The C2 domain in its typical version (PKC-C2) is a β-sandwich composed of 8 β-strands. References1. ^{{cite journal|last1=Kister|first1=A. E.|last2=Fokas|first2=A. S.|last3=Papatheodorou|first3=T. S.|last4=Gelfand|first4=I. M.|title=Strict rules determine arrangements of strands in sandwich proteins |journal=PNAS| date=2006| volume=103| issue=11| pages=4107–4110| doi=10.1073/pnas.0510747103| pmid=16537492| pmc=1449654}} 1 : Protein structural motifs |
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