Factor XII: Difference between revisions
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<StructureSection load='7fbp' size='340' side='right' caption='Glycosylated human factor XII protease domain ( | <StructureSection load='7fbp' size='340' side='right' caption='Glycosylated human factor XII protease domain (deep sky blue) complex with cyclic peptide inhibitor (green)' scene='91/916250/Cv/2'> | ||
== Function == | == Function == | ||
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== Relevance == | == Relevance == | ||
Inhibition of the FXII-driven contact system may be a promising therapeutic anticoagulation treatment strategy<ref>PMID:27834692</ref>. | 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> | The 3D structure of the complex between human FXIIa and a cyclic peptide inhibitor<ref>PMID:34723512</ref> shows the peptide forming <scene name='91/916250/Cv/6'>intermolecular β-sheet-like hydrogen bonds with FXIIa at two regions</scene>. Contacting residues of human FXIIa and cyclic peptide inhibitor are shown at ball-and-stick representation and colored deep sky blue and green, respectively. <scene name='91/916250/Cv/7'>Another representation</scene> of the complex between human FXIIa and a cyclic peptide inhibitor. | ||
==FXII 3D structures== | ==FXII 3D structures== | ||