Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations

Biochemistry. 1993 Jan 12;32(1):282-9. doi: 10.1021/bi00052a036.

Abstract

The pairing of the cysteines in disulfide bonds was investigated for the 68-residue RGD-containing protein kistrin, a potent antagonist of the integrin GP IIbIIIa and an inhibitor of platelet aggregation. Kistrin belongs to a family of homologous proteins found in snake venoms termed disintegrins, all of which have a cysteine content. The disulfide pairing of the 12 cysteines was investigated by chemical analysis, NMR spectroscopy, and distance geometry calculations. The data show that the disulfide pairs are 4-19, 6-14, 13-36, 27-33, 32-57, and 45-64. The various means for assigning the disulfide bonds are described, and the results are compared with the cysteine pairings reported for other disintegrin proteins.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Chemical Phenomena
  • Chemistry, Physical
  • Crotalid Venoms / chemistry
  • Cysteine / chemistry*
  • Disulfides / chemistry
  • Endopeptidases / metabolism
  • Intercellular Signaling Peptides and Proteins
  • Magnetic Resonance Spectroscopy*
  • Molecular Sequence Data
  • Molecular Structure
  • Peptide Fragments / chemistry
  • Peptides / chemistry*
  • Platelet Aggregation Inhibitors / chemistry*
  • Platelet Membrane Glycoproteins / antagonists & inhibitors*
  • Protein Structure, Secondary
  • Viper Venoms / chemistry

Substances

  • Crotalid Venoms
  • Disulfides
  • Intercellular Signaling Peptides and Proteins
  • Peptide Fragments
  • Peptides
  • Platelet Aggregation Inhibitors
  • Platelet Membrane Glycoproteins
  • Viper Venoms
  • echistatin
  • kistrin
  • Endopeptidases
  • Cysteine