1e9b: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,097 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,097 edits
No edit summary
Line 1: Line 1:
[[Image:1e9b.jpg|left|200px]]
{{Seed}}
[[Image:1e9b.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1e9b|  PDB=1e9b  |  SCENE=  }}  
{{STRUCTURE_1e9b|  PDB=1e9b  |  SCENE=  }}  


'''HUMAN THYMIDYLATE KINASE COMPLEXED WITH AZTMP AND APPNP'''
===HUMAN THYMIDYLATE KINASE COMPLEXED WITH AZTMP AND APPNP===




==Overview==
<!--
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.
The line below this paragraph, {{ABSTRACT_PUBMED_11071809}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 11071809 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_11071809}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: P-loop]]
[[Category: P-loop]]
[[Category: Thymidylate kinase]]
[[Category: Thymidylate kinase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:49:35 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:21:21 2008''
Retrieved from "https://proteopedia.org/1e9b"