1dan
From Proteopedia
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[[Image:1dan.gif|left|200px]]<br /> | [[Image:1dan.gif|left|200px]]<br /> | ||
<applet load="1dan" size="450" color="white" frame="true" align="right" spinBox="true" | <applet load="1dan" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1dan" /> | + | caption="1dan, resolution 2.00Å" /> |
| - | ''''''<br /> | + | '''COMPLEX OF ACTIVE SITE INHIBITED HUMAN BLOOD COAGULATION FACTOR VIIA WITH HUMAN RECOMBINANT SOLUBLE TISSUE FACTOR'''<br /> |
==Overview== | ==Overview== | ||
Blood coagulation is initiated when tissue factor binds to coagulation, factor VIIa to give an enzymatically active complex which then activates, factors IX and X, leading to thrombin generation and clot formation. We, have determined the crystal structure at 2.0-A degrees resolution of, active-site-inhibited factor VIIa complexed with the cleaved extracellular, domain of tissue factor. In the complex, factor VIIa adopts an extended, conformation. This structure provides a basis for understanding many, molecular aspects of the initiation of coagulation. | Blood coagulation is initiated when tissue factor binds to coagulation, factor VIIa to give an enzymatically active complex which then activates, factors IX and X, leading to thrombin generation and clot formation. We, have determined the crystal structure at 2.0-A degrees resolution of, active-site-inhibited factor VIIa complexed with the cleaved extracellular, domain of tissue factor. In the complex, factor VIIa adopts an extended, conformation. This structure provides a basis for understanding many, molecular aspects of the initiation of coagulation. | ||
| + | |||
| + | ==Disease== | ||
| + | Known diseases associated with this structure: Esophageal squamous cell carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606551 606551]], Factor VII deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=227500 227500]], Myocardial infarction, decreased susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=227500 227500]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 1DAN is a | + | 1DAN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BGC, FUC, CA, CAC, CL and CH2 as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1DAN with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb75_1.html Tissue Factor]]. Active as [http://en.wikipedia.org/wiki/Coagulation_factor_VIIa Coagulation factor VIIa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.21 3.4.21.21] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DAN OCA]. |
==Reference== | ==Reference== | ||
The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor., Banner DW, D'Arcy A, Chene C, Winkler FK, Guha A, Konigsberg WH, Nemerson Y, Kirchhofer D, Nature. 1996 Mar 7;380(6569):41-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8598903 8598903] | The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor., Banner DW, D'Arcy A, Chene C, Winkler FK, Guha A, Konigsberg WH, Nemerson Y, Kirchhofer D, Nature. 1996 Mar 7;380(6569):41-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8598903 8598903] | ||
| + | [[Category: Coagulation factor VIIa]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| Line 22: | Line 26: | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: FUC]] | [[Category: FUC]] | ||
| + | [[Category: blood coagulation]] | ||
| + | [[Category: co-factor]] | ||
| + | [[Category: complex]] | ||
| + | [[Category: complex (serine protease/cofactor/ligand)]] | ||
| + | [[Category: egf]] | ||
| + | [[Category: gla]] | ||
| + | [[Category: inhibitor]] | ||
| + | [[Category: receptor enzyme]] | ||
| + | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:30:38 2007'' |
Revision as of 14:24, 12 November 2007
|
COMPLEX OF ACTIVE SITE INHIBITED HUMAN BLOOD COAGULATION FACTOR VIIA WITH HUMAN RECOMBINANT SOLUBLE TISSUE FACTOR
Contents |
Overview
Blood coagulation is initiated when tissue factor binds to coagulation, factor VIIa to give an enzymatically active complex which then activates, factors IX and X, leading to thrombin generation and clot formation. We, have determined the crystal structure at 2.0-A degrees resolution of, active-site-inhibited factor VIIa complexed with the cleaved extracellular, domain of tissue factor. In the complex, factor VIIa adopts an extended, conformation. This structure provides a basis for understanding many, molecular aspects of the initiation of coagulation.
Disease
Known diseases associated with this structure: Esophageal squamous cell carcinoma OMIM:[606551], Factor VII deficiency OMIM:[227500], Myocardial infarction, decreased susceptibility to OMIM:[227500]
About this Structure
1DAN is a Protein complex structure of sequences from Homo sapiens with BGC, FUC, CA, CAC, CL and CH2 as ligands. The following page contains interesting information on the relation of 1DAN with [Tissue Factor]. Active as Coagulation factor VIIa, with EC number 3.4.21.21 Full crystallographic information is available from OCA.
Reference
The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor., Banner DW, D'Arcy A, Chene C, Winkler FK, Guha A, Konigsberg WH, Nemerson Y, Kirchhofer D, Nature. 1996 Mar 7;380(6569):41-6. PMID:8598903
Page seeded by OCA on Mon Nov 12 16:30:38 2007
Categories: Coagulation factor VIIa | Homo sapiens | Protein complex | Tissue Factor | Banner, D.W. | BGC | CA | CAC | CH2 | CL | FUC | Blood coagulation | Co-factor | Complex | Complex (serine protease/cofactor/ligand) | Egf | Gla | Inhibitor | Receptor enzyme | Serine protease
