1kim

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kim.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1kim.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kim| PDB=1kim | SCENE= }}
{{STRUCTURE_1kim| PDB=1kim | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE I COMPLEXED WITH DEOXYTHYMIDINE'''
+
===CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE I COMPLEXED WITH DEOXYTHYMIDINE===
-
==Overview==
+
<!--
-
Antiherpes therapies are principally targeted at viral thymidine kinases and utilize nucleoside analogs, the triphosphates of which are inhibitors of viral DNA polymerase or result in toxic effects when incorporated into DNA. The most frequently used drug, aciclovir (Zovirax), is a relatively poor substrate for thymidine kinase and high-resolution structural information on drugs and other molecules binding to the target is therefore important for the design of novel and more potent chemotherapy, both in antiherpes treatment and in gene therapy systems where thymidine kinase is expressed. Here, we report for the first time the binary complexes of HSV-1 thymidine kinase (TK) with the drug molecules aciclovir and penciclovir, determined by X-ray crystallography at 2.37 A resolution. Moreover, from new data at 2.14 A resolution, the refined structure of the complex of TK with its substrate deoxythymidine (R = 0.209 for 96% of all data) now reveals much detail concerning substrate and solvent interactions with the enzyme. Structures of the complexes of TK with four halogen-containing substrate analogs have also been solved, to resolutions better than 2.4 A. The various TK inhibitors broadly fall into three groups which together probe the space of the enzyme active site in a manner that no one molecule does alone, so giving a composite picture of active site interactions that can be exploited in the design of novel compounds.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9715911}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9715911 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9715911}}
==About this Structure==
==About this Structure==
Line 41: Line 45:
[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Viridae]]
[[Category: Viridae]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:47:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:23:52 2008''

Revision as of 07:23, 2 July 2008

Image:1kim.png

Template:STRUCTURE 1kim

CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE I COMPLEXED WITH DEOXYTHYMIDINE

Template:ABSTRACT PUBMED 9715911

About this Structure

1KIM is a Single protein structure of sequence from Human herpesvirus 1. This structure supersedes the now removed PDB entry 1kin. Full crystallographic information is available from OCA.

Reference

Exploring the active site of herpes simplex virus type-1 thymidine kinase by X-ray crystallography of complexes with aciclovir and other ligands., Champness JN, Bennett MS, Wien F, Visse R, Summers WC, Herdewijn P, de Clerq E, Ostrowski T, Jarvest RL, Sanderson MR, Proteins. 1998 Aug 15;32(3):350-61. PMID:9715911

Page seeded by OCA on Wed Jul 2 10:23:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kim"
Personal tools