6wvh: Difference between revisions
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<StructureSection load='6wvh' size='340' side='right'caption='[[6wvh]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='6wvh' size='340' side='right'caption='[[6wvh]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6wvh]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6wvh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WVH 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]] 1.99Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=UA7:Brodifacoum'>UA7</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6wvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wvh OCA], [https://pdbe.org/6wvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wvh RCSB], [https://www.ebi.ac.uk/pdbsum/6wvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wvh ProSAT]</span></td></tr> | |||
< | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Disease == | |||
[https://www.uniprot.org/uniprot/VKOR1_HUMAN VKOR1_HUMAN] Prediction of resistance to vitamin K antagonists;Prediction of toxicity or dose selection of vitamin K antagonists;Hereditary combined deficiency of vitamin K-dependent clotting factors. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/K0NYR4_9CAUD K0NYR4_9CAUD] [https://www.uniprot.org/uniprot/VKOR1_HUMAN VKOR1_HUMAN] Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development.<ref>PMID:14765194</ref> <ref>PMID:14765195</ref> <ref>PMID:15879509</ref> <ref>PMID:16270630</ref> <ref>PMID:20978134</ref> <ref>PMID:22923610</ref> <ref>PMID:33154105</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6wvh" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6wvh" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aequorea victoria]] | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Li W]] | |||
[[Category: Li | [[Category: Liu S]] | ||
[[Category: Liu | [[Category: Sukumar N]] | ||
[[Category: Sukumar | |||
Revision as of 17:37, 18 October 2023
Human VKOR with BrodifacoumHuman VKOR with Brodifacoum
Structural highlights
DiseaseVKOR1_HUMAN Prediction of resistance to vitamin K antagonists;Prediction of toxicity or dose selection of vitamin K antagonists;Hereditary combined deficiency of vitamin K-dependent clotting factors. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. FunctionK0NYR4_9CAUD VKOR1_HUMAN Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development.[1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedVitamin K antagonists are widely used anticoagulants targeting vitamin K epoxide reductases (VKOR), a family of integral membrane enzymes. To elucidate their catalytic cycle and inhibitory mechanism, here we report eleven x-ray crystal structures of human VKOR and pufferfish VKOR-like with substrates and antagonists in different redox states. Substrates entering the active site in a partially oxidized state form a cysteine adduct that induces an open-to-closed conformational change, triggering reduction. Binding and catalysis is facilitated by hydrogen-bonding interactions in a hydrophobic pocket. The antagonists bind specifically to the same hydrogen-bonding residues and induce a similar closed conformation. Thus, vitamin K antagonists act through mimicking the key interactions and conformational changes required for the VKOR catalytic cycle. Structural basis of antagonizing the vitamin K catalytic cycle for anticoagulation.,Liu S, Li S, Shen G, Sukumar N, Krezel AM, Li W Science. 2020 Nov 5. pii: science.abc5667. doi: 10.1126/science.abc5667. PMID:33154105[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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