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2bfr

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{{STRUCTURE_2bfr| PDB=2bfr | SCENE= }}
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'''THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE'''
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===THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE===
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==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}}
==About this Structure==
==About this Structure==
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[[Category: Macro_h2a domain/hydrolase]]
[[Category: Macro_h2a domain/hydrolase]]
[[Category: Nucleotide]]
[[Category: Nucleotide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:13:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:33:01 2008''

Revision as of 14:33, 28 July 2008

Image:2bfr.png

Template:STRUCTURE 2bfr

THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE

Template:ABSTRACT PUBMED 15902274

About this Structure

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

Reference

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

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