2bfr: Difference between revisions

Revision as of 17:33, 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:2bfr.png

Template:STRUCTURE 2bfr

THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULETHE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE

Template:ABSTRACT PUBMED 15902274

About this StructureAbout this Structure

2BFR 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 17:33:01 2008

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

OCA

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-'''THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE'''
+===THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE===
-==Overview==
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-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.
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+{{ABSTRACT_PUBMED_15902274}}
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 [[Category: Macro_h2a domain/hydrolase]]
 [[Category: Nucleotide]]
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