Publication Abstract from PubMed
Rattlesnake 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
