Factor XII

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(New page: <StructureSection load='7fbp' size='340' side='right' caption='Glycosylated human factor XII protease domain (grey) complex with cyclic peptide inhibitor (green)' scene=''> This is a def...)
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<StructureSection load='7fbp' size='340' side='right' caption='Glycosylated human factor XII protease domain (grey) complex with cyclic peptide inhibitor (green)' scene=''>
<StructureSection load='7fbp' size='340' side='right' caption='Glycosylated human factor XII protease domain (grey) complex with cyclic peptide inhibitor (green)' scene=''>
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This is a default text for your page '''Factor XII'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
 
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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.
 
== Function ==
== Function ==
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Coagulation '''factor XII''' (FXII) or '''Hageman factor''' is the zymogen of '''factor XIIa''' (FXIIa). Factor XIIa , the active form of factor XII, is of crucial importance in fibrin formation<ref>PMID:22993391</ref> and initiates the procoagulant and proinflammatory contact system.
== Disease ==
== Disease ==
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FXIIa has critical role in coagulation in thromboembolic diseases.
== Relevance ==
== Relevance ==
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Inhibition of the FXII-driven contact system may be a promising therapeutic anticoagulation treatment strategy<ref>PMID:27834692</ref>. The choice of cyclic peptides as inhibitors of FXIIa is based on their being cell-permeable and more stable to proteolysis.
== Structural highlights ==
== Structural highlights ==
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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.
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The 3D structure of the complex between human FXIIa and a cyclic peptide inhibitor<ref>PMID:34723512</ref>.shows the peptide forming intermolecular β-sheet-like hydrogen bonds with FXIIa at two regions.
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==FXII 3D structures==
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[[3D structures of FXII]]
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</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>
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[[Category:Topic Page]]

Revision as of 08:02, 29 June 2022

Glycosylated human factor XII protease domain (grey) complex with cyclic peptide inhibitor (green)

Drag the structure with the mouse to rotate

References

  1. ↑ Renne T, Schmaier AH, Nickel KF, Blomback M, Maas C. In vivo roles of factor XII. Blood. 2012 Nov 22;120(22):4296-303. doi: 10.1182/blood-2012-07-292094. Epub 2012, Sep 19. PMID:22993391 doi:http://dx.doi.org/10.1182/blood-2012-07-292094
  2. ↑ Nickel KF, Long AT, Fuchs TA, Butler LM, Renne T. Factor XII as a Therapeutic Target in Thromboembolic and Inflammatory Diseases. Arterioscler Thromb Vasc Biol. 2017 Jan;37(1):13-20. doi:, 10.1161/ATVBAHA.116.308595. Epub 2016 Nov 10. PMID:27834692 doi:http://dx.doi.org/10.1161/ATVBAHA.116.308595
  3. ↑ Liu W, de Veer SJ, Huang YH, Sengoku T, Okada C, Ogata K, Zdenek CN, Fry BG, Swedberg JE, Passioura T, Craik DJ, Suga H. An Ultrapotent and Selective Cyclic Peptide Inhibitor of Human beta-Factor XIIa in a Cyclotide Scaffold. J Am Chem Soc. 2021 Nov 10;143(44):18481-18489. doi: 10.1021/jacs.1c07574. Epub, 2021 Nov 1. PMID:34723512 doi:http://dx.doi.org/10.1021/jacs.1c07574

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel

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