1sdd: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1sdd |SIZE=350|CAPTION= <scene name='initialview01'>1sdd</scene>, resolution 2.8Å | |PDB= 1sdd |SIZE=350|CAPTION= <scene name='initialview01'>1sdd</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1czv|1CZV]], [[1czt|1CZT]], [[1czs|1CZS]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sdd OCA], [http://www.ebi.ac.uk/pdbsum/1sdd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sdd RCSB]</span> | |||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Hockin, M F.]] | [[Category: Hockin, M F.]] | ||
[[Category: Mann, K G.]] | [[Category: Mann, K G.]] | ||
[[Category: coagulation]] | [[Category: coagulation]] | ||
[[Category: cofactor]] | [[Category: cofactor]] | ||
[[Category: copper-binding protein]] | [[Category: copper-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:40:31 2008'' | ||
Revision as of 23:40, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1CZV, 1CZT, 1CZS
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Bovine Factor Vai
OverviewOverview
In vertebrate hemostasis, factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation compared with factor Xa alone. Structurally, little is known about the mechanism by which factor Va alters catalysis within this complex. Here, we report a crystal structure of protein C inactivated factor Va (A1.A3-C1-C2) that depicts a previously uncharacterized domain arrangement. This orientation has implications for binding to membranes essential for function. A high-affinity calcium-binding site and a copper-binding site have both been identified. Surprisingly, neither shows a direct involvement in chain association. This structure represents the largest physiologically relevant fragment of factor Va solved to date and provides a new scaffold for the future generation of models of coagulation cofactors.
About this StructureAbout this Structure
1SDD is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function., Adams TE, Hockin MF, Mann KG, Everse SJ, Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8918-23. Epub 2004 Jun 7. PMID:15184653
Page seeded by OCA on Sun Mar 30 23:40:31 2008