Factor IXa: Difference between revisions
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James Nolan (talk | contribs) New page: ==Structure== <StructureSection load='6mv4' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for your page '''Factor IXa'''. Click above on '''... |
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==Structure== | ==Structure== | ||
<StructureSection load='6mv4' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='6mv4' size='340' side='right' caption='Caption for this structure' scene=''> | ||
The crystal structure of Factor IXa complexed with p-amino-benzamidine.<ref>PMID:30725510</ref> | The crystal structure of Factor IXa complexed with p-amino-benzamidine.<ref>PMID:30725510</ref> | ||
== Function == | == Function == | ||
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
The catalytic triad at the active site is comprised of | Here is an <scene name='84/845969/Cat_triad_over/1'>Overview of the Catalytic Triad</scene>The catalytic triad at the active site is comprised of His57, Asp102 and Ser1985 is highlighted. Now <scene name='84/845969/Cat_triad_zoom/1'>Zoom in on the Catalytic Triad</scene>. The His borrows an H from Her, which now attacks at the substrate. In this case the active site is blocked by the inhibitor, p-amino-benzamidine. | ||
Mutation of C252S results in Hemophilia B, probably due to destabilization of the loop including the His of the catalytic triad. | Mutation of C252S results in Hemophilia B, probably due to destabilization of the loop including the His of the catalytic triad. | ||
A mutation of T194A exhibits increased activity and stability and appears to enhance the risk for Deep Vein Thrombosis and stroke. | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 10:06, 10 February 2021
Structure
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