Order out of complexity--protein structures that interact with heparin.
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.
Mulloy
B
B
Laboratory for Molecular Structure, National Institute for Biological Standards and Control, Hertfordshire, UK. bmulloy@nibsc.ac.uk
Linhardt
R J
RJ
D017304:Annexin A5 / Q000737:chemistry; D023181:Antimicrobial Cationic Peptides; D000991:Antithrombins / Q000737:chemistry; D001798:Blood Proteins / Q000737:chemistry*; D002240:Carbohydrate Sequence; D002352:Carrier Proteins / Q000737:chemistry*; D005346:Fibroblast Growth Factors / Q000737:chemistry; D006493:Heparin / Q000737:chemistry*; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D014764:Viral Proteins / Q000737:chemistry
C062991:AZU1 protein, human; D017304:Annexin A5; D023181:Antimicrobial Cationic Peptides; D000991:Antithrombins; D001798:Blood Proteins; D002352:Carrier Proteins; D046911:Macromolecular Substances; D014764:Viral Proteins; D005346:Fibroblast Growth Factors; D006493:Heparin