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6wvb
From Proteopedia
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<StructureSection load='6wvb' size='340' side='right'caption='[[6wvb]], [[Resolution|resolution]] 2.87Å' scene=''> | <StructureSection load='6wvb' size='340' side='right'caption='[[6wvb]], [[Resolution|resolution]] 2.87Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <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 [https://proteopedia.org/fgij/fg.htm?mol=6WVB 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]] 2.872Å</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=SWF:S-WARFARIN'>SWF</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=6wvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wvb OCA], [https://pdbe.org/6wvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wvb RCSB], [https://www.ebi.ac.uk/pdbsum/6wvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wvb ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</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. | ||
| - | + | ==See Also== | |
| - | + | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Aeqvi]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Li | + | [[Category: Li W]] |
| - | [[Category: Liu | + | [[Category: Liu S]] |
| - | [[Category: Sukumar | + | [[Category: Sukumar N]] |
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Current revision
Takifugu rubripes VKOR-like with warfarin
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Categories: Large Structures | Li W | Liu S | Sukumar N
