2rf5: Difference between revisions

Revision as of 00:47, 29 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:2rf5.png

Template:STRUCTURE 2rf5

Crystal structure of human tankyrase 1- catalytic PARP domainCrystal structure of human tankyrase 1- catalytic PARP domain

Template:ABSTRACT PUBMED 18436240

About this StructureAbout this Structure

2RF5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Zinc binding catalytic domain of human tankyrase 1., Lehtio L, Collins R, van den Berg S, Johansson A, Dahlgren LG, Hammarstrom M, Helleday T, Holmberg-Schiavone L, Karlberg T, Weigelt J, J Mol Biol. 2008 May 23;379(1):136-45. Epub 2008 Apr 3. PMID:18436240

Page seeded by OCA on Tue Jul 29 00:47:23 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2rf5.jpg|left|200px]]
+{{Seed}}
+[[Image:2rf5.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2rf5|  PDB=2rf5  |  SCENE=  }}
-'''Crystal structure of human tankyrase 1- catalytic PARP domain'''
+===Crystal structure of human tankyrase 1- catalytic PARP domain===
-==Overview==
+<!--
-Tankyrases are recently discovered proteins implicated in many important functions in the cell including telomere homeostasis and mitosis. Tankyrase modulates the activity of target proteins through poly(ADP-ribosyl)ation, and here we report the structure of the catalytic poly(ADP-ribose) polymerase (PARP) domain of human tankyrase 1. This is the first structure of a PARP domain from the tankyrase subfamily. The present structure reveals that tankyrases contain a short zinc-binding motif, which has not been predicted. Tankyrase activity contributes to telomere elongation observed in various cancer cells and tankyrase inhibition has been suggested as a potential route for cancer therapy. In comparison with other PARPs, significant structural differences are observed in the regions lining the substrate-binding site of tankyrase 1. These findings will be of great value to facilitate structure-based design of selective PARP inhibitors, in general, and tankyrase inhibitors, in particular.
+The line below this paragraph, {{ABSTRACT_PUBMED_18436240}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18436240 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18436240}}
 ==About this Structure==
@@ Line 75: / Line 79: @@
 [[Category: Translocation]]
 [[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun  4 09:59:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 00:47:23 2008''