1p75

From Proteopedia

(Difference between revisions)

Revision as of 11:47, 7 February 2016

Crystal structure of EHV4-TK complexed with TP5A

Structural highlights

1p75 is a 4 chain structure with sequence from Ehv-4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1p72, 1p6x, 1p73, 1p7c
Gene:	TK (EHV-4)
Activity:	Thymidine kinase, with EC number 2.7.1.21
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[KITH_EHV4] In latent infection, may allow the virus to be reactivated and to grow in cells lacking a high concentration of phosphorylated nucleic acid precursors, such as nerve cells that do not replicate their genome (By similarity).

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 PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p75"

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     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1p75 ConSurf].
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1p75

From Proteopedia

Revision as of 11:47, 7 February 2016

Crystal structure of EHV4-TK complexed with TP5A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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