2bfq: Difference between revisions

Revision as of 10:45, 28 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:2bfq.png

Template:STRUCTURE 2bfq

MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULESMACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES

Template:ABSTRACT PUBMED 15902274

About this StructureAbout this Structure

2BFQ is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

ReferenceReference

The macro domain is an ADP-ribose binding module., Karras GI, Kustatscher G, Buhecha HR, Allen MD, Pugieux C, Sait F, Bycroft M, Ladurner AG, EMBO J. 2005 Jun 1;24(11):1911-20. Epub 2005 May 19. PMID:15902274

Page seeded by OCA on Mon Jul 28 10:45:02 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2bfq.gif|left|200px]]
+{{Seed}}
+[[Image:2bfq.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2bfq|  PDB=2bfq  |  SCENE=  }}
-'''MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES'''
+===MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES===
-==Overview==
+<!--
-The ADP-ribosylation of proteins is an important post-translational modification that occurs in a variety of biological processes, including DNA repair, transcription, chromatin biology and long-term memory formation. Yet no protein modules are known that specifically recognize the ADP-ribose nucleotide. We provide biochemical and structural evidence that macro domains are high-affinity ADP-ribose binding modules. Our structural analysis reveals a conserved ligand binding pocket among the macro domain fold. Consistently, distinct human macro domains retain their ability to bind ADP-ribose. In addition, some macro domain proteins also recognize poly-ADP-ribose as a ligand. Our data suggest an important role for proteins containing macro domains in the biology of ADP-ribose.
+The line below this paragraph, {{ABSTRACT_PUBMED_15902274}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15902274 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15902274}}
 ==About this Structure==
@@ Line 34: / Line 38: @@
 [[Category: Macro_h2a domain/hydrolase]]
 [[Category: Nucleotide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:13:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:45:02 2008''