6ojv
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human thymidylate synthase delta(7-29) in complex with dUMP and 2-amino-4-oxo-4,7-dihydro-pyrrolo[2,3-d]pyrimidine-methyl-phenyl-L-glutamic acid== | |
| + | <StructureSection load='6ojv' size='340' side='right'caption='[[6ojv]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ojv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OJV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OJV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2XB:N-{4-[(2-AMINO-4-HYDROXY-7H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)METHYL]BENZOYL}-L-GLUTAMIC+ACID'>2XB</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</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=6ojv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ojv OCA], [http://pdbe.org/6ojv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ojv RCSB], [http://www.ebi.ac.uk/pdbsum/6ojv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ojv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TYSY_HUMAN TYSY_HUMAN]] Contributes to the de novo mitochondrial thymidylate biosynthesis pathway.<ref>PMID:21876188</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Thymidylate synthase (TS), found in all organisms, is an essential enzyme responsible for the de novo synthesis of deoxythymidine monophosphate. The TS active sites of the protozoal parasite Cryptosporidium hominis and human are relatively conserved. Evaluation of antifolate compound 1 and its R-enantiomer 2 against both enzymes reveals divergent inhibitor selectivity and enzyme stereospecificity. To establish how C. hominis and human TS (ChTS and hTS) selectively discriminate 1 and 2, respectively, we determined crystal structures of ChTS complexed with 2 and hTS complexed with 1 or 2. Coupled with the previously determined structure of ChTS complexed with 1, we discuss a possible mechanism for enzyme stereospecificity and inhibitor selectivity. This article is protected by copyright. All rights reserved. | ||
| - | + | Understanding the Structural Basis of Species Selective, Stereospecific Inhibition for Cryptosporidium and Human Thymidylate Synthase.,Czyzyk DJ, Valhondo M, Jorgensen WL, Anderson KS FEBS Lett. 2019 Jun 7. doi: 10.1002/1873-3468.13474. PMID:31172516<ref>PMID:31172516</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6ojv" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Anderson, K S]] | ||
| + | [[Category: Czyzyk, D J]] | ||
| + | [[Category: Jorgensen, W L]] | ||
[[Category: Valhondo, M]] | [[Category: Valhondo, M]] | ||
| - | [[Category: | + | [[Category: Inhibitor]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | [[Category: | + | [[Category: Transferase-transferase inhibitor complex]] |
| + | [[Category: Ts-dhfr]] | ||
Revision as of 06:09, 19 June 2019
Crystal structure of human thymidylate synthase delta(7-29) in complex with dUMP and 2-amino-4-oxo-4,7-dihydro-pyrrolo[2,3-d]pyrimidine-methyl-phenyl-L-glutamic acid
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