1MUQ

X-ray Crystal Structure of Rattlesnake Venom Complexed With Thiodigalactoside

Summary for 1MUQ

• Entry DOI: 10.2210/pdb1muq/pdb
• Related: 1JZN
• Related PRD ID: PRD_900027
• Descriptor: Galactose-specific lectin, 1-thio-beta-D-galactopyranose-(1-1)-beta-D-galactopyranose, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: c-type lectin, protein-carbohydrate complex, decamer, calcium binding, sugar binding protein
• Biological source: Crotalus atrox (western diamondback rattlesnake)
• Total number of polymer chains: 5
• Total formula weight: 82776.05

Authors

Walker, J.R.,Nagar, B.,Young, N.M.,Hirama, T.,Rini, J.M. (deposition date: 2002-09-24, release date: 2003-07-01, Last modification date: 2024-11-20)

Primary citation

Walker, J.R.,Nagar, B.,Young, N.M.,Hirama, T.,Rini, J.M.
X-ray Crystal Structure of a Galactose-Specific C-Type Lectin Possessing a Novel Decameric Quaternary Structure.
Biochemistry, 43:3783-3792, 2004

PubMed Abstract: 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.

PubMed: 15049685
DOI: 10.1021/bi035871a

Experimental method

X-RAY DIFFRACTION (2.3 Å)