Antithrombin-binding oligosaccharides: structural diversities in a unique function?

被引：24
|
作者：
Guerrini, Marco [1 ]
Mourier, Pierre A. J. [2 ]
Torri, Giangiacomo [1 ]
Viskov, Christian [2 ]
机构：
[1] Ist Ric Chim & Biochim G Ronzoni, I-20133 Milan, Italy
[2] Sanofi, F-94403 Vitry Sur Seine, France
来源：
GLYCOCONJUGATE JOURNAL | 2014年 / 31卷 / 6-7期
关键词：
Antithrombin; Heparin; Oligosaccharides; NMR; Protein-ligand interaction; MOLECULAR-WEIGHT HEPARINS; FIBROBLAST GROWTH-FACTORS; ANTI-FACTOR-XA; CHEMOENZYMATIC SYNTHESIS; ANTICOAGULANT ACTIVITIES; HIGH-AFFINITY; PENTASACCHARIDE; CONFORMATION; NMR; SEQUENCE;
D O I：
10.1007/s10719-014-9543-9
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：409 / 416
页数：8
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