Conformation of heparin pentasaccharide bound to antithrombin III

Biochemical Journal

Volumn 359, Issue 2, 2001, Pages 265-272

  Hricovini M ^a   Guerrini, M ^a   Bisio, A ^a   Torri, G ^a   Petitou, M ^a   Casu, B ^a  

^a INSTITUTE OF CHEMISTRY   (Slovakia)

Author keywords

NMR spectroscopy; Protein carbohydrate interaction; Solution structure

Indexed keywords

CARBOXYLIC ACIDS; GEOMETRY; OPTIMIZATION; PROTEINS; SACCHARIFICATION; SOLUTIONS;

HEPARIN PENTASACCHARIDE BOUND;

BIOCHEMISTRY;

ANTITHROMBIN III; GLUCOSAMINE DERIVATIVE; GLUCURONIC ACID; GLYCOSIDE; IDURONIC ACID; PENTASACCHARIDE;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; CARBOHYDRATE ANALYSIS; CONFORMATIONAL TRANSITION; GEOMETRY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN INTERACTION; STRUCTURE ANALYSIS;

ANTITHROMBIN III; BINDING SITES; CARBOHYDRATE CONFORMATION; CARBOHYDRATE SEQUENCE; HEPARIN; MACROMOLECULAR SUBSTANCES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OLIGOSACCHARIDES; PROTEIN BINDING; PROTEIN CONFORMATION; SOLUTIONS;

EID: 0035886931     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3590265     Document Type: Article

References (32)

1. Glycosaminoglycans and the regulation of blood coagulation
2. Structure and biological interactions of heparin and heparan sulphate
3. Structure-activity relationship in heparin: A synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity
4. The unique antithrombin III binding domain of heparin: A lead to new synthetic antithrombotics
5. Conformation of the pentasaccharide corresponding to the binding site of heparin for antithrombin III
6. Dynamics in aqueous solutions of the pentasaccharide corresponding to the binding site of heparin for antithrombin III studied by NMR relaxation measurements
7. Controversial glycosaminoglycan conformations
8. Controversial glycosaminoglycan conformations
9. Conformer populations of L-iduronic acid residues in glycosaminoglycan sequences
10. Conformational analysis of synthetic heparin-like oligosaccharides containing α-L-idopyranosyluronic acid
11. Evidence for conformational equilibrium of the sulphated L-iduronate residue in heparin and in synthetic heparin mono- and oligosaccharides: NMR and force-field studies
12. Conformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
13. Heparin structure and interactions with basic fibroblast growth factor
14. Conformation of the pentasaccharide corresponding to the binding site of heparin for antithrombin III
15. Structure of heparin derived tetrasaccharide complexed to the plasma protein antithrombin derived from NOEs, J-couplings and chemical shifts
16. The anticoagulant activation of antithrombin by heparin
17. Macro model V 5.0
18. A mechanism for heparin-induced potentiation of antithrombin III
19. Complete relaxation and conformational exchange matrix (CORCEMA) analysis of NOESY spectra of interacting systems; two-dimensional transferred NOESY
20. The oligosaccharide side chain on Asn-135 of α-antithrombin, absent in β antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change
21. NMR molecular modelling studies of the solution conformation of heparin
22. Pyranose ring flexibility. Mapping of physical data for iduronate in continuous conformational space
23. Conformation and dynamics of heparin and heparan sulphate
24. Role of arginine 129 in heparin binding activation of antithrombin
25. The role of Arg 46 and Arg 47 of antithrombin in heparin binding
26. Interaction of heparin and antithrombin III
27. A new, highly potent, heparin-like pentasaccharide fragment containing a glucose residue instead of a glucosamine
28. Synthesis of a conformationally constrained heparin-like pentasaccharide
29. Containing heparin pentasaccharide to probe the conformation of the antithrombin III binding sequence
30. Sugars slide into heparin activity
31. Synthesis of thrombin-inhibiting heparin mimetics without side effects