1e9c

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[[Image:1e9c.jpg|left|200px]]
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{{STRUCTURE_1e9c| PDB=1e9c | SCENE= }}
{{STRUCTURE_1e9c| PDB=1e9c | SCENE= }}
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'''MUTANT HUMAN THYMIDYLATE KINASE COMPLEXED WITH TMP AND APPNP'''
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===MUTANT HUMAN THYMIDYLATE KINASE COMPLEXED WITH TMP AND APPNP===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 11071809 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11071809}}
==About this Structure==
==About this Structure==
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[[Category: P-loop]]
[[Category: P-loop]]
[[Category: Thymidylate kinase]]
[[Category: Thymidylate kinase]]
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Revision as of 21:21, 30 June 2008

Image:1e9c.png

Template:STRUCTURE 1e9c

MUTANT HUMAN THYMIDYLATE KINASE COMPLEXED WITH TMP AND APPNP

Template:ABSTRACT PUBMED 11071809

About this Structure

1E9C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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