Factor IXa - Revision history

Michal Harel at 10:06, 10 February 2021

2021-02-10T10:06:44Z

← Older revision		Revision as of 10:06, 10 February 2021
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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=''>
	~~This is a default text for your page '''Factor IXa'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.~~
	~~You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.~~
	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 ==

James Nolan at 18:32, 19 May 2020

2020-05-19T18:32:55Z

← Older revision		Revision as of 18:32, 19 May 2020
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	== Structural highlights ==		== Structural highlights ==

	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.~~Zoom in on~~ the Catalytic Triad</scene>.		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 ~~His41~~, ~~Asp89~~ and ~~Ser185~~ is highlighted.		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.		A mutation of T194A exhibits increased activity and stability and appears to enhance the risk for Deep Vein Thrombosis and stroke.

James Nolan at 18:23, 19 May 2020

2020-05-19T18:23:31Z

← Older revision		Revision as of 18:23, 19 May 2020
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	== Structural highlights ==		== Structural highlights ==

	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.Zoom in on the Catalytic Triad</scene>.
	The catalytic triad at the active site is comprised of His41, Asp89 and Ser185 is highlighted.		The catalytic triad at the active site is comprised of His41, Asp89 and Ser185 is highlighted.
	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/>

James Nolan: New page: ==Structure== This is a default text for your page '''Factor IXa'''. Click above on '''...

2020-05-19T15:09:02Z

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 '''...

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 '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
The crystal structure of Factor IXa complexed with p-amino-benzamidine.<ref>PMID:30725510</ref>
== Function ==
The Factor IX protein is a serine protease that is part of the blood coagulation cascade.
== Disease ==
Defects in the F9 gene, coding for Factor IX, result in the disease Hemophilia B. The F9 gene is located on the X chromosome. Hemophilia B is distinct from Hemophilia A, which results from defects in the F8 gene coding for Factor VIII, also located on the X chromosome. Factor IXa (the activated, clipped form of Factor IX) interacts with Factor VIIIa to form an active protease, which intern clips Factor X to its active form, Factor Xa.
== Relevance ==

== Structural highlights ==

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 His41, Asp89 and Ser185 is highlighted.
Mutation of C252S results in Hemophilia B, probably due to destabilization of the loop including the His of the catalytic triad.

</StructureSection>
== References ==
<references/>