1e2h: Difference between revisions

Revision as of 00:02, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1e2h.png

1e2h, resolution 1.90Å ()

Ligands:

Activity:

Thymidine kinase, with EC number 2.7.1.21

Related:

1kim, 1vtk, 2vtk, 3vtk, 1ki2, 1ki4, 1ki5, 1ki6, 1ki7, 1ki8, 1e2i, 1e2j, 1e2k, 1e2l, 1e2m, 1e2n, 1e2p

Structural annotation:
Resources:	CATH : 1E2Ha00, 1E2Hb00 InterPro : Ipr001889 Pfam : PF00693 SCOP : d1e2ha_, d1e2hb_ UniProt : P03176

Functional annotation:
Biological process:	TMP biosynthetic process DNA replication
Molecular function:	kinase activity ATP binding transferase activity thymidine kinase activity nucleotide binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

THE NUCLEOSIDE BINDING SITE OF HERPES SIMPLEX TYPE 1 THYMIDINE KINASE ANALYZED BY X-RAY CRYSTALLOGRAPHYTHE NUCLEOSIDE BINDING SITE OF HERPES SIMPLEX TYPE 1 THYMIDINE KINASE ANALYZED BY X-RAY CRYSTALLOGRAPHY

Template:ABSTRACT PUBMED 11056041

About this StructureAbout this Structure

1E2H is a Single protein structure of sequence from Human herpesvirus 1. Full crystallographic information is available from OCA.

ReferenceReference

Nucleoside binding site of herpes simplex type 1 thymidine kinase analyzed by X-ray crystallography., Vogt J, Perozzo R, Pautsch A, Prota A, Schelling P, Pilger B, Folkers G, Scapozza L, Schulz GE, Proteins. 2000 Dec 1;41(4):545-53. PMID:11056041

Page seeded by OCA on Tue Jul 1 00:02:23 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1e2h|  PDB=1e2h  |  SCENE=  }}
-'''THE NUCLEOSIDE BINDING SITE OF HERPES SIMPLEX TYPE 1 THYMIDINE KINASE ANALYZED BY X-RAY CRYSTALLOGRAPHY'''
+===THE NUCLEOSIDE BINDING SITE OF HERPES SIMPLEX TYPE 1 THYMIDINE KINASE ANALYZED BY X-RAY CRYSTALLOGRAPHY===
-==Overview==
+<!--
-The crystal structures of the full-length Herpes simplex virus type 1 thymidine kinase in its unligated form and in a complex with an adenine analogue have been determined at 1.9 A resolution. The unligated enzyme contains four water molecules in the thymidine pocket and reveals a small induced fit on substrate binding. The structure of the ligated enzyme shows for the first time a bound adenine analogue after numerous complexes with thymine and guanine analogues have been reported. The adenine analogue constitutes a new lead compound for enzyme-prodrug gene therapy. In addition, the structure of mutant Q125N modifying the binding site of the natural substrate thymidine in complex with this substrate has been established at 2.5 A resolution. It reveals that neither the binding mode of thymidine nor the polypeptide backbone conformation is altered, except that the two major hydrogen bonds to thymidine are replaced by a single water-mediated hydrogen bond, which improves the relative acceptance of the prodrugs aciclovir and ganciclovir compared with the natural substrate. Accordingly, the mutant structure represents a first step toward improving the virus-directed enzyme-prodrug gene therapy by enzyme engineering.
+The line below this paragraph, {{ABSTRACT_PUBMED_11056041}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11056041 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11056041}}
 ==About this Structure==
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 [[Category: Thymidine kinase]]
 [[Category: X-ray crystallography]]
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