1muq

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1muq, resolution 2.30Å

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X-ray Crystal Structure of Rattlesnake Venom Complexed With Thiodigalactoside

Overview

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.

About this Structure

1MUQ is a Single protein structure of sequence from Crotalus atrox with GAL, CA, NA and TDG as ligands. Full crystallographic information is available from OCA.

Reference

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

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