4xde: Difference between revisions
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==Coagulation Factor XII protease domain crystal structure== | ==Coagulation Factor XII protease domain crystal structure== | ||
<StructureSection load='4xde' size='340' side='right' caption='[[4xde]], [[Resolution|resolution]] 2.14Å' scene=''> | <StructureSection load='4xde' size='340' side='right'caption='[[4xde]], [[Resolution|resolution]] 2.14Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xde]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XDE OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4xde]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XDE FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4xde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xde OCA], [https://pdbe.org/4xde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xde RCSB], [https://www.ebi.ac.uk/pdbsum/4xde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xde ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
[ | [https://www.uniprot.org/uniprot/FA12_HUMAN FA12_HUMAN] Congenital factor XII deficiency;Hereditary angioedema type 3. Defects in F12 are the cause of factor XII deficiency (FA12D) [MIM:[https://omim.org/entry/234000 234000]; also known as Hageman factor deficiency. This trait is an asymptomatic anomaly of in vitro blood coagulation. Its diagnosis is based on finding a low plasma activity of the factor in coagulating assays. It is usually only accidentally discovered through pre-operative blood tests. F12 deficiency is divided into two categories, a cross-reacting material (CRM)-negative group (negative F12 antigen detection) and a CRM-positive group (positive F12 antigen detection).<ref>PMID:8528215</ref> <ref>PMID:2882793</ref> <ref>PMID:2510163</ref> <ref>PMID:8049433</ref> <ref>PMID:9354665</ref> <ref>PMID:10361128</ref> <ref>PMID:11776307</ref> <ref>PMID:15205584</ref> <ref>PMID:15617741</ref> Defects in F12 are the cause of hereditary angioedema type 3 (HAE3) [MIM:[https://omim.org/entry/610618 610618]; also known as estrogen-related HAE or hereditary angioneurotic edema with normal C1 inhibitor concentration and function. HAE is characterized by episodic local subcutaneous edema, and submucosal edema involving the upper respiratory and gastrointestinal tracts. HAE3 occurs exclusively in women and is precipitated or worsened by high estrogen levels (e.g. during pregnancy or treatment with oral contraceptives). It differs from HAE types 1 and 2 in that both concentration and function of C1 inhibitor are normal.<ref>PMID:16638441</ref> <ref>PMID:17186468</ref> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FA12_HUMAN FA12_HUMAN] Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa.<ref>PMID:21304106</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4xde" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[3D structures of FXII|3D structures of FXII]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Awford | [[Category: Large Structures]] | ||
[[Category: Dekker | [[Category: Awford J]] | ||
[[Category: Dreveny | [[Category: Dekker LV]] | ||
[[Category: Emsley | [[Category: Dreveny I]] | ||
[[Category: Fisher | [[Category: Emsley J]] | ||
[[Category: Li | [[Category: Fisher PM]] | ||
[[Category: Pathak | [[Category: Li C]] | ||
[[Category: Wilmann | [[Category: Pathak M]] | ||
[[Category: Wilmann P]] | |||