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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== 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== | ||
Latest revision as of 17:37, 4 July 2022
FunctionCoagulation 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[1] and initiates the procoagulant and proinflammatory contact system. DiseaseFXIIa has critical role in coagulation in thromboembolic diseases. RelevanceInhibition of the FXII-driven contact system may be a promising therapeutic anticoagulation treatment strategy[2]. The choice of cyclic peptides as inhibitors of FXIIa is based on their being cell-permeable and more stable to proteolysis. Structural highlightsThe 3D structure of the complex between human FXIIa and a cyclic peptide inhibitor[3] shows the peptide forming . Contacting residues of human FXIIa and cyclic peptide inhibitor are shown at ball-and-stick representation and colored deep sky blue and green, respectively. of the complex between human FXIIa and a cyclic peptide inhibitor. FXII 3D structures
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ReferencesReferences
- ↑ 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
- ↑ 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
- ↑ 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