1p72

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{{STRUCTURE_1p72| PDB=1p72 | SCENE= }}
{{STRUCTURE_1p72| PDB=1p72 | SCENE= }}
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'''Crystal structure of EHV4-TK complexed with Thy and ADP'''
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===Crystal structure of EHV4-TK complexed with Thy and ADP===
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==Overview==
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Crystal structures of equine herpesvirus type-4 thymidine kinase (EHV4-TK) in complex with (i). thymidine and ADP, (ii). thymidine and SO(4) and the bisubstrate analogs, (iii). TP(4)A, and (iv). TP(5)A have been solved. Additionally, the structure of herpes simplex virus type-1 thymidine kinase (HSV1-TK) in complex with TP(5)A has been determined. These are the first structures of nucleoside kinases revealing conformational transitions upon binding of bisubstrate analogs. The structural basis for the dual thymidine and thymidylate kinase activity of these TKs is elucidated. While the active sites of HSV1-TK and EHV4-TK resemble one another, notable differences are observed in the Lid regions and in the way the enzymes bind the base of the phosphoryl-acceptor. The latter difference could partly explain the higher activity of EHV4-TK toward the prodrug ganciclovir.
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(as it appears on PubMed at http://www.pubmed.gov), where 14527394 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14527394}}
==About this Structure==
==About this Structure==
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[[Category: Lid]]
[[Category: Lid]]
[[Category: P-loop]]
[[Category: P-loop]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:17:02 2008''

Revision as of 06:17, 28 July 2008

Image:1p72.png

Template:STRUCTURE 1p72

Crystal structure of EHV4-TK complexed with Thy and ADP

Template:ABSTRACT PUBMED 14527394

About this Structure

1P72 is a Single protein structure of sequence from Equid herpesvirus 4. Full crystallographic information is available from OCA.

Reference

Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases., Gardberg A, Shuvalova L, Monnerjahn C, Konrad M, Lavie A, Structure. 2003 Oct;11(10):1265-77. PMID:14527394

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