title: Antithrombin-binding oligosaccharides: structural diversities in a unique function?
abstract: Heparin-antithrombin interaction is one of the most documented examples of heparin/protein complexes. The specific heparin sequence responsible for the binding corresponds to a pentasaccharide sequence with an internal 3-O-sulfated glucosamine residue. Moreover, the position of the pentasaccharide along the chain as well as the structure of the neighbor units affects the affinity to antithrombin. The development of separation and purification techniques, in conjunction with physico-chemical approaches (mostly NMR), allowed to characterize several structural variants of antithrombin-binding oligosaccharides, both in the free state and in complex with antithrombin. The article provides an overview of the studies that lead to the elucidation of the mechanism of interaction as well as acquiring new knowledge in heparin biosynthesis.
authors.affiliation: Istituto di Ricerche Chimiche e Biochimiche "G. Ronzoni", via G. Colombo 81, 20133, Milan, Italy, guerrini@ronzoni.it.
authors.forename: Marco
authors.initials: M
authors.lastname: Guerrini
authors.forename: Pierre A J
authors.initials: PA
authors.lastname: Mourier
authors.forename: Giangiacomo
authors.initials: G
authors.lastname: Torri
authors.forename: Christian
authors.initials: C
authors.lastname: Viskov
mesh_terms: D000991:Antithrombins / Q000378:metabolism*; D002236:Carbohydrate Conformation; D009682:Magnetic Resonance Spectroscopy; D009844:Oligosaccharides / Q000737:chemistry / Q000378:metabolism*; D020349:Surface Plasmon Resonance
chemical_list: D000991:Antithrombins; D009844:Oligosaccharides