1e9c

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{{STRUCTURE_1e9c| PDB=1e9c | SCENE= }}
 
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===Mutant human thymidylate kinase complexed with TMP and APPNP===
 
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{{ABSTRACT_PUBMED_11071809}}
 
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==About this Structure==
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==Mutant human thymidylate kinase complexed with TMP and APPNP==
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[[1e9c]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9C OCA].
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<StructureSection load='1e9c' size='340' side='right'caption='[[1e9c]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1e9c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E9C FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TMP:THYMIDINE-5-PHOSPHATE'>TMP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9c OCA], [https://pdbe.org/1e9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e9c RCSB], [https://www.ebi.ac.uk/pdbsum/1e9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e9c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KTHY_HUMAN KTHY_HUMAN] Catalyzes the conversion of dTMP to dTDP.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e9/1e9c_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e9c ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The 60-fold reduced phosphorylation rate of azidothymidine (AZT) monophosphate (AZTMP), the partially activated AZT metabolite, by human thymidylate kinase (TMPK) severely limits the efficacy of this anti-HIV prodrug. Crystal structures of different TMPK nucleotide complexes indicate that steric hindrance by the azido group of AZTMP prevents formation of the catalytically active closed conformation of the P-loop of TMPK. The F105Y mutant and a chimeric mutant that contains sequences of the human and Escherichia coli enzyme phosphorylate AZTMP 20-fold faster than the wild-type enzyme. The structural basis of the increased activity is assigned to stabilization of the closed P-loop conformation.
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==See Also==
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Potentiating AZT activation: structures of wild-type and mutant human thymidylate kinase suggest reasons for the mutants' improved kinetics with the HIV prodrug metabolite AZTMP.,Ostermann N, Lavie A, Padiyar S, Brundiers R, Veit T, Reinstein J, Goody RS, Konrad M, Schlichting I J Mol Biol. 2000 Nov 17;304(1):43-53. PMID:11071809<ref>PMID:11071809</ref>
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*[[Thymidylate kinase|Thymidylate kinase]]
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:011071809</ref><references group="xtra"/><references/>
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</div>
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[[Category: Human]]
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<div class="pdbe-citations 1e9c" style="background-color:#fffaf0;"></div>
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[[Category: DTMP kinase]]
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[[Category: Brundiers, R.]]
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==See Also==
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[[Category: Goody, R S.]]
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*[[Thymidylate kinase 3D structures|Thymidylate kinase 3D structures]]
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[[Category: Konrad, M.]]
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== References ==
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[[Category: Lavie, A.]]
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<references/>
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[[Category: Ostermann, N.]]
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__TOC__
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[[Category: Padiyar, S.]]
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</StructureSection>
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[[Category: Reintein, J.]]
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[[Category: Homo sapiens]]
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[[Category: Schlichting, I.]]
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[[Category: Large Structures]]
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[[Category: Veit, T.]]
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[[Category: Brundiers R]]
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[[Category: P-loop]]
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[[Category: Goody RS]]
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[[Category: Phosphotransferase]]
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[[Category: Konrad M]]
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[[Category: Thymidylate kinase]]
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[[Category: Lavie A]]
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[[Category: Transferase]]
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[[Category: Ostermann N]]
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[[Category: Padiyar S]]
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[[Category: Reintein J]]
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[[Category: Schlichting I]]
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[[Category: Veit T]]

Current revision

Mutant human thymidylate kinase complexed with TMP and APPNP

PDB ID 1e9c

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