Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist

Science. 1991 Jul 26;253(5018):445-8. doi: 10.1126/science.1862345.

Abstract

The structure of kistrin, which is a member of a homologous family of glycoprotein IIb-IIIa (GP IIb-IIIa) antagonists and potent protein inhibitors of platelet aggregation, has been determined by two-dimensional nuclear magnetic resonance (NMR) spectroscopy. The 68-residue protein consists of a series of tightly packed loops held together by six disulfide bonds and has almost no regular secondary structure. Kistrin has an Arg-Gly-Asp (RGD) adhesion site recognition sequence important for binding to GP IIb-IIIa that is located at the apex of a long loop across the surface of the protein.

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
  • Glycoproteins / chemistry*
  • Humans
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptides / chemistry*
  • Peptides / genetics
  • Platelet Aggregation Inhibitors / chemistry*
  • Platelet Membrane Glycoproteins / antagonists & inhibitors*
  • Protein Conformation

Substances

  • Glycoproteins
  • Peptides
  • Platelet Aggregation Inhibitors
  • Platelet Membrane Glycoproteins
  • kistrin