1muq
From Proteopedia
X-ray Crystal Structure of Rattlesnake Venom Complexed With Thiodigalactoside
Structural highlights
FunctionLECG_CROAT Galactose-binding protein which recognizes specific carbohydrate structures and agglutinates a variety of animal cells by binding to cell-surface glycoproteins and glycolipids. Calcium-dependent lectin. Shows high hemagglutinating activity (MHC is 10 ng/ml) (PubMed:1989986).[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRattlesnake venom lectin (RSL) from the western diamondback rattlesnake (Crotalus atrox) is an oligomeric galactose-specific C-type lectin. The X-ray crystal structure of RSL, in complex with lactose and thiodigalactoside, at 2.2 and 2.3 A resolution, respectively, reveals a decameric protein composed of two 5-fold symmetric pentamers arranged in a staggered, back-to-back orientation. Each monomer corresponds to a single canonical C-type lectin carbohydrate recognition domain devoid of accessory domains and is disulfide-bonded to a monomer in the other pentamer. The structure is the first example of that of a carbohydrate complex of a vertebrate galactose-specific C-type lectin. The 10 carbohydrate-binding sites, located on the rim of the decamer, suggest a role for multivalent interactions and a mechanism for RSL's ability to promote receptor cross-linking and cell aggregation. X-ray crystal structure of a galactose-specific C-type lectin possessing a novel decameric quaternary structure.,Walker JR, Nagar B, Young NM, Hirama T, Rini JM Biochemistry. 2004 Apr 6;43(13):3783-92. PMID:15049685[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Crotalus atrox | Large Structures | Hirama T | Nagar B | Rini JM | Walker JR | Young NM
