title: Order out of complexity--protein structures that interact with heparin.
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.
authors.affiliation: Laboratory for Molecular Structure, National Institute for Biological Standards and Control, Hertfordshire, UK. bmulloy@nibsc.ac.uk
authors.forename: B
authors.initials: B
authors.lastname: Mulloy
authors.forename: R J
authors.initials: RJ
authors.lastname: Linhardt
mesh_terms: 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
chemical_list: 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