6oah
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human FPPS in complex with an allosteric inhibitor YF-02-78== | |
| + | <StructureSection load='6oah' size='340' side='right'caption='[[6oah]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6oah]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OAH FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=M2V:[(1R)-1-{[6-(3-chloro-4-methylphenyl)thieno[2,3-d]pyrimidin-4-yl]amino}-2-phenylethyl]phosphonic+acid'>M2V</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6oah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oah OCA], [http://pdbe.org/6oah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oah RCSB], [http://www.ebi.ac.uk/pdbsum/6oah PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oah ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FPPS_HUMAN FPPS_HUMAN]] Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Thienopyrimidine-based allosteric inhibitors of the human farnesyl pyrophosphate synthase (hFPPS), characterized by a chiral alpha-aminophosphonic acid moiety, were synthesized as enantiomerically enriched pairs, and their binding mode was investigated by X-ray crystallography. A general consensus in the binding orientation of all (R)- and (S)-enantiomers was revealed. This finding is a prerequisite for establishing a reliable structure-activity relationship (SAR) model. | ||
| - | + | Chirality-Driven Mode of Binding of alpha-Aminophosphonic Acid-Based Allosteric Inhibitors of the Human Farnesyl Pyrophosphate Synthase (hFPPS).,Feng Y, Park J, Li SG, Boutin R, Viereck P, Schilling MA, Berghuis AM, Tsantrizos YS J Med Chem. 2019 Oct 16. doi: 10.1021/acs.jmedchem.9b01104. PMID:31577901<ref>PMID:31577901</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6oah" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Berghuis, A M]] | ||
[[Category: Park, J]] | [[Category: Park, J]] | ||
| - | [[Category: | + | [[Category: Transferase]] |
| + | [[Category: Transferase-transferase inhibitor complex]] | ||
Revision as of 06:45, 6 November 2019
Crystal structure of human FPPS in complex with an allosteric inhibitor YF-02-78
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