X-ray crystal structure of a galactose-specific C-type lectin possessing a novel decameric quaternary structure

Biochemistry. 2004 Apr 6;43(13):3783-92. doi: 10.1021/bi035871a.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Calcium / chemistry
  • Carbohydrates / chemistry
  • Crotalid Venoms / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Disulfides / chemistry
  • Galactose / chemistry*
  • Lactose / chemistry
  • Lectins, C-Type / chemistry*
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Quaternary*
  • Sequence Homology, Amino Acid
  • Surface Plasmon Resonance
  • Thiogalactosides / chemistry


  • Carbohydrates
  • Crotalid Venoms
  • Disulfides
  • Lectins, C-Type
  • Thiogalactosides
  • thiodigalactoside
  • Lactose
  • Calcium
  • Galactose

Associated data

  • PDB/1JZN
  • PDB/1MUQ