Document Detail

Crystal structure of cleaved bovine antithrombin III at 3.2 A resolution.
MedLine Citation:
PMID:  8331659     Owner:  NLM     Status:  MEDLINE    
The crystal structure of cleaved antithrombin III (ATIII) has been determined to 3.2 A resolution by single isomorphous replacement, real space density modification and phase extension protocols. The heavy-atom sites and the first molecular envelope were determined owing to the molecular replacement solution previously reported and partially refined. Refinement of the two molecules of the asymmetric unit led to a crystallographic R-factor of 0.212 for all reflections between 8.0 and 3.2 A, without inclusion of water molecules. The root-mean-square deviation from ideal values is, respectively, 0.015 A and 3.6 degrees for bond lengths and bond angles. The topology of the molecule closely resembles that of cleaved serpins inhibitors with the two residues forming the reactive bond at opposite ends of the molecule. The most significant difference between ATIII and alpha 1-antitrypsin lies in the 45 residue N-terminal extension in ATIII which contribute to the definition of the heparin binding site. This loop region at the surface of the molecule is held by two disulphide bridges to the protein core and exhibits high temperature factor values. It forms a valley which restrains the possibilities for binding of heparin. Docking of the pentasaccharide unit which represents the minimum fragment of heparin able to bind to ATIII indicates a possible role for arginine 14 in the interaction of heparin and the protein.
L Mourey; J P Samama; M Delarue; M Petitou; J Choay; D Moras
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of molecular biology     Volume:  232     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  1993 Jul 
Date Detail:
Created Date:  1993-08-19     Completed Date:  1993-08-19     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  223-41     Citation Subset:  IM    
UPR de Biologie Structurale Institut de Biologie, Moléculaire et Cellulaire du CNRS, Strasbourg, France.
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MeSH Terms
Amino Acid Sequence
Antithrombin III / ultrastructure*
Carbohydrate Sequence
Computer Simulation
Models, Molecular
Molecular Sequence Data
Oligosaccharides / chemistry
Peptide Fragments
Protein Processing, Post-Translational
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Alignment
X-Ray Diffraction
Reg. No./Substance:
0/Disulfides; 0/Oligosaccharides; 0/Peptide Fragments; 9000-94-6/Antithrombin III

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