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| - | [[Image:1cvw.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1cvw| PDB=1cvw | SCENE= }} | | {{STRUCTURE_1cvw| PDB=1cvw | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF ACTIVE SITE-INHIBITED HUMAN COAGULATION FACTOR VIIA (DES-GLA)'''
| + | ===CRYSTAL STRUCTURE OF ACTIVE SITE-INHIBITED HUMAN COAGULATION FACTOR VIIA (DES-GLA)=== |
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| - | ==Overview==
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| - | Factor VIIa (FVIIa) is a crucial haemostatic protease consisting of four distinct domains termed the Gla, epidermal growth factor-1 (EGF-1), EGF-2, and protease domains (from N- to C-terminus). The crystal structure of human FVIIa inhibited at the active site with 1, 5-dansyl-Glu-Gly-Arg-chloromethyl ketone and lacking the Gla domain has been solved to a resolution of 2.28 A. The EGF-2 and protease domains were well resolved, whereas no electron density for the EGF-1 domain was observed, suggesting a flexible arrangement or disorder within the crystal. Superposition of the protease domain of the present structure with that previously resolved in the tissue factor (TF)/FVIIai complex revealed that although overall the domain structures are similar, the EGF-2 domain is rotated by 7.5 degrees relative to the protease domain on binding TF. A single cleavage in the protease domain was found, between Arg315 and Lys316 (chymotrypsin numbering 170C-170D) in a FVII-specific insertion loop: this cleavage appeared to be essential for crystallisation. Insertion of the heavy chain N-terminal Ile153 is essentially identical in the two structures, as is the geometry of the active site residues and the inhibitor C-terminal arginine residue. Some differences are seen in the cleaved loop, but changes in TF-contact residues are generally minor. This structure supports the hypothesis that TF binding enables spatial domain arrangements in the flexible FVIIa molecule necessary for procoagulant function and furthermore that active site occupancy induces FVIIa active conformation via N-terminal insertion.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10544046}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10544046 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10544046}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Inhibitor]] | | [[Category: Inhibitor]] |
| | [[Category: Serine protease]] | | [[Category: Serine protease]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:09:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:32:32 2008'' |
Revision as of 18:32, 30 June 2008
Template:STRUCTURE 1cvw
CRYSTAL STRUCTURE OF ACTIVE SITE-INHIBITED HUMAN COAGULATION FACTOR VIIA (DES-GLA)
Template:ABSTRACT PUBMED 10544046
About this Structure
1CVW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of active site-inhibited human coagulation factor VIIa (des-Gla)., Kemball-Cook G, Johnson DJ, Tuddenham EG, Harlos K, J Struct Biol. 1999 Oct;127(3):213-23. PMID:10544046
Page seeded by OCA on Mon Jun 30 21:32:32 2008
