1dan
From Proteopedia
(New page: 100px <applet load="1dan" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dan, 2.00 Å " /> '''Complex Of Active Site Inhibited H...) |
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- | [[Image:1dan.gif|left|100px]] | ||
- | <applet load="1dan" size="450" color="white" frame="true" align="right" spinBox="true" | ||
- | caption="1dan, 2.00 Å " /> | ||
- | '''Complex Of Active Site Inhibited Human Blood Coagulation Factor Viia With Human Recombinant Soluble Tissue Factor'''<br /> | ||
- | Bound ligands : [[BGC]],[[CA]],[[CAC]],[[CGU]],[[CH2]],[[CL]],[[DPN]],[[FUC]] <br /> | ||
+ | <applet load="1dan" size="300" color="white" frame="true" align="right" spinBox="true" caption="1DAN " /> | ||
+ | '''Complex Of Active Site Inhibited Human Blood Coagulation Factor Viia With Human Recombinant Soluble Tissue Factor''' | ||
==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. | ||
- | == | + | ==Functional features== |
- | + | ==Structural features== | |
- | + | ==PDB entry information== | |
- | + | '''Author:''' [[D.W.Banner]] | |
- | == | + | |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + | ||
+ | ==Crystal information== | ||
+ | <TABLE border=1><tr> | ||
+ | <td><FONT COLOR=#006600>length a</font></td> | ||
+ | <td><FONT COLOR=#006600>length b</font></td> | ||
+ | <td><FONT COLOR=#006600>length c</font></td> | ||
+ | <td><FONT COLOR=#006600>angle alpha</font></td> | ||
+ | <td><FONT COLOR=#006600>angle beta</font></td> | ||
+ | <td><FONT COLOR=#006600>angle gamma</font></td> | ||
+ | </tr> <tr> | ||
+ | <TD align=right>70.650</td> | ||
+ | <TD align=right>82.550</td> | ||
+ | <TD align=right>126.500</td> | ||
+ | <TD align=right>90.00</td> | ||
+ | <TD align=right>90.00</td> | ||
+ | <TD align=right>90.00</td></tr> | ||
+ | </TABLE> | ||
==Related Structures== | ==Related Structures== | ||
by [http://bioinfo.tg.fh-giessen.de/pdbselect/README homologous] chain: [http://bip.weizmann.ac.il//oca-bin/ocashort?id=1JPS 1JPS], [http://bip.weizmann.ac.il//oca-bin/ocashort?id=1KLI 1KLI], [http://bip.weizmann.ac.il//oca-bin/ocashort?id=1YGC 1YGC], [http://bip.weizmann.ac.il//oca-bin/ocashort?id=1Z6J 1Z6J] | by [http://bioinfo.tg.fh-giessen.de/pdbselect/README homologous] chain: [http://bip.weizmann.ac.il//oca-bin/ocashort?id=1JPS 1JPS], [http://bip.weizmann.ac.il//oca-bin/ocashort?id=1KLI 1KLI], [http://bip.weizmann.ac.il//oca-bin/ocashort?id=1YGC 1YGC], [http://bip.weizmann.ac.il//oca-bin/ocashort?id=1Z6J 1Z6J] | ||
- | ==Links== | ||
- | [http://ispc.weizmann.ac.il:80/oca-bin/ocashort?id=1DAN 1dan at OCA]<br /> | ||
- | This structure was featured in Molecule of the Month [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb75_1.html pdb75]<br /> | ||
- | ==References== | ||
- | #'''Primary:''' Banner DW, D'Arcy A, Chene C, Winkler FK, Guha A, Konigsberg WH, Nemerson Y, Kirchhofer D "The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor." <i>Nature 1996 Mar 7;380(6569):41-6.</i> [http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8598903 PMID:8598903] | ||
- | [[Category: D.W.Banner]] | ||
- | [[Category: BGC]] | ||
- | [[Category: CA]] | ||
- | [[Category: CAC]] | ||
- | [[Category: CGU]] | ||
- | [[Category: CH2]] | ||
- | [[Category: CL]] | ||
- | [[Category: DPN]] | ||
- | [[Category: FUC]] | ||
- | [[Category: F3 (Gene)]] | ||
- | [[Category: F7 (Gene)]] | ||
- | [[Category: Coagulation Factor Iii (Disease)]] | ||
- | [[Category: Myocardial infarction (Disease)]] | ||
- | [[Category: Homo sapiens]] | ||
- | [[Category: H: (SCOP_Domain)]] | ||
- | [[Category: L:1-48 (SCOP_Domain)]] | ||
- | [[Category: L:49-86 (SCOP_Domain)]] | ||
- | [[Category: L:87-142 (SCOP_Domain)]] | ||
- | [[Category: T:,U:91-106 (SCOP_Domain)]] | ||
- | [[Category: U:107-210 (SCOP_Domain)]] | ||
- | [[Category: 49267 (SCOP_Family)]] | ||
- | [[Category: 50550 (SCOP_Family)]] | ||
- | [[Category: 57201 (SCOP_Family)]] | ||
- | [[Category: 57632 (SCOP_Family)]] | ||
- | [[Category: 49266 (SCOP_SuperFamily)]] | ||
- | [[Category: 50514 (SCOP_SuperFamily)]] | ||
- | [[Category: 57197 (SCOP_SuperFamily)]] | ||
- | [[Category: 57631 (SCOP_SuperFamily)]] | ||
- | [[Category: 48725 (SCOP_Fold)]] | ||
- | [[Category: 50493 (SCOP_Fold)]] | ||
- | [[Category: 57015 (SCOP_Fold)]] | ||
- | [[Category: 57629 (SCOP_Fold)]] | ||
- | [[Category: 48724 (SCOP_Class)]] | ||
- | [[Category: 56992 (SCOP_Class)]] | ||
- | ''Page seeded by [http://bip.weizmann.ac.il/oca OCA ] on Thu Oct 25 | + | ''Page seeded by [http://bip.weizmann.ac.il/oca OCA ] on Thu Oct 25 10:20:37 2007'' |
Revision as of 08:16, 25 October 2007
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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.
Functional features
Structural features
PDB entry information
Author: D.W.Banner
Crystal information
length a | length b | length c | angle alpha | angle beta | angle gamma |
70.650 | 82.550 | 126.500 | 90.00 | 90.00 | 90.00 |
Related Structures
by homologous chain: 1JPS, 1KLI, 1YGC, 1Z6J
Page seeded by OCA on Thu Oct 25 10:20:37 2007