Order out of complexity--protein structures that interact with heparin

Curr Opin Struct Biol. 2001 Oct;11(5):623-8. doi: 10.1016/s0959-440x(00)00257-8.

Abstract

Many proteins of widely differing functionality and structure are capable of binding heparin. Structural characterisations of the many types of such complexes are being reported in ever-increasing number and at improved resolution. Several crystal structures of complexes formed through the interaction of heparin-derived oligosaccharides with one or more protein partners have been described.

Publication types

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

MeSH terms

  • Annexin A5 / chemistry
  • Antimicrobial Cationic Peptides
  • Antithrombins / chemistry
  • Blood Proteins / chemistry*
  • Carbohydrate Sequence
  • Carrier Proteins / chemistry*
  • Fibroblast Growth Factors / chemistry
  • Heparin / chemistry*
  • Macromolecular Substances
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Viral Proteins / chemistry

Substances

  • AZU1 protein, human
  • Annexin A5
  • Antimicrobial Cationic Peptides
  • Antithrombins
  • Blood Proteins
  • Carrier Proteins
  • Macromolecular Substances
  • Viral Proteins
  • Fibroblast Growth Factors
  • Heparin