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==Takifugu rubripes VKOR-like with warfarin== | ==Takifugu rubripes VKOR-like with warfarin== | ||
<StructureSection load='6wvb' size='340' side='right'caption='[[6wvb]]' scene=''> | <StructureSection load='6wvb' size='340' side='right'caption='[[6wvb]], [[Resolution|resolution]] 2.87Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WVB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WVB FirstGlance]. <br> | <table><tr><td colspan='2'>[[6wvb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WVB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WVB FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wvb OCA], [http://pdbe.org/6wvb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wvb RCSB], [http://www.ebi.ac.uk/pdbsum/6wvb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wvb ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SWF:S-WARFARIN'>SWF</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gfp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 AEQVI])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wvb OCA], [http://pdbe.org/6wvb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wvb RCSB], [http://www.ebi.ac.uk/pdbsum/6wvb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wvb ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vitamin 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<ref>PMID:33154105</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6wvb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aeqvi]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Li W]] | [[Category: Li, W]] | ||
[[Category: Liu S]] | [[Category: Liu, S]] | ||
[[Category: Sukumar N]] | [[Category: Sukumar, N]] | ||
[[Category: Membrane protein]] | |||
[[Category: Vitamin k epoxide reductase]] | |||
[[Category: Vkor]] | |||
[[Category: Vkor-like protein]] | |||
[[Category: Vkorl]] | |||
Revision as of 10:11, 25 November 2020
Takifugu rubripes VKOR-like with warfarinTakifugu rubripes VKOR-like with warfarin
Structural highlights
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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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