Factor XII: Difference between revisions
Michal Harel (talk | contribs) 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=''> | ||
== Function == | == Function == | ||
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 == | ||
FXIIa has critical role in coagulation in thromboembolic diseases. | |||
== Relevance == | == Relevance == | ||
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 == | ||
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. | |||
==FXII 3D structures== | |||
[[3D structures of FXII]] | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] |