|
|
| Line 1: |
Line 1: |
| [[Image:1sdd.gif|left|200px]] | | {{Seed}} |
| | [[Image:1sdd.png|left|200px]] |
|
| |
|
| <!-- | | <!-- |
| Line 9: |
Line 10: |
| {{STRUCTURE_1sdd| PDB=1sdd | SCENE= }} | | {{STRUCTURE_1sdd| PDB=1sdd | SCENE= }} |
|
| |
|
| '''Crystal Structure of Bovine Factor Vai'''
| | ===Crystal Structure of Bovine Factor Vai=== |
|
| |
|
|
| |
|
| ==Overview==
| | <!-- |
| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15184653}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15184653 is the PubMed ID number. |
| | --> |
| | {{ABSTRACT_PUBMED_15184653}} |
|
| |
|
| ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| [[Category: Cofactor]] | | [[Category: Cofactor]] |
| [[Category: Copper-binding protein]] | | [[Category: Copper-binding protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:34:21 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:25:44 2008'' |