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