Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains

Nature. 1994 Feb 10;367(6463):532-8. doi: 10.1038/367532a0.

Abstract

The three-dimensional structure of the ligand-binding region of human E-selectin has been determined at 2.0 A resolution. The structure reveals limited contact between the two domains and a coordination of Ca2+ not predicted from other C-type lectins. Structure/function analysis indicates a defined region and specific amino-acid side chains that may be involved in ligand binding. These features of the E-selectin/ligand interaction have important implications for understanding the recruitment of leukocytes to sites of inflammation.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / metabolism
  • Animals
  • CHO Cells
  • Carrier Proteins / metabolism
  • Cell Adhesion
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / metabolism*
  • Cricetinae
  • Crystallography, X-Ray
  • E-Selectin
  • Epidermal Growth Factor / metabolism*
  • Humans
  • Lectins / metabolism
  • Lewis X Antigen / chemistry
  • Ligands
  • Mannose-Binding Lectins
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis
  • Neutrophils / metabolism
  • Rats
  • Structure-Activity Relationship

Substances

  • Amino Acids
  • Carrier Proteins
  • Cell Adhesion Molecules
  • E-Selectin
  • Lectins
  • Lewis X Antigen
  • Ligands
  • Mannose-Binding Lectins
  • Epidermal Growth Factor