1e9a: Difference between revisions
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<StructureSection load='1e9a' size='340' side='right'caption='[[1e9a]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1e9a' size='340' side='right'caption='[[1e9a]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e9a]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1e9a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E9A FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=Z5A:P1-(5-ADENOSYL)P5-(5-(3AZIDO-3-DEOXYTHYMIDYL))PENTAPHOSPHATE'>Z5A</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=Z5A:P1-(5-ADENOSYL)P5-(5-(3AZIDO-3-DEOXYTHYMIDYL))PENTAPHOSPHATE'>Z5A</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e2d|1e2d]], [[1e2e|1e2e]], [[1e2f|1e2f]], [[1e2g|1e2g]], [[1e2q|1e2q]], [[1e98|1e98]], [[1e99|1e99]], [[1e9b|1e9b]], [[1e9c|1e9c]], [[1e9d|1e9d]], [[1e9e|1e9e]], [[1e9f|1e9f]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e2d|1e2d]], [[1e2e|1e2e]], [[1e2f|1e2f]], [[1e2g|1e2g]], [[1e2q|1e2q]], [[1e98|1e98]], [[1e99|1e99]], [[1e9b|1e9b]], [[1e9c|1e9c]], [[1e9d|1e9d]], [[1e9e|1e9e]], [[1e9f|1e9f]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/dTMP_kinase dTMP kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.9 2.7.4.9] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9a OCA], [https://pdbe.org/1e9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e9a RCSB], [https://www.ebi.ac.uk/pdbsum/1e9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e9a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 30: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Thymidylate kinase|Thymidylate kinase]] | *[[Thymidylate kinase 3D structures|Thymidylate kinase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 08:46, 28 April 2021
Human thymidylate kinase complexed with the bisubstrate inhibitor AZTP5AHuman thymidylate kinase complexed with the bisubstrate inhibitor AZTP5A
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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