2bfq

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[[Category: nucleotide]]
[[Category: nucleotide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:45:15 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:36:29 2007''

Revision as of 14:31, 30 October 2007


2bfq, resolution 1.5Å

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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.

About this Structure

2BFQ is a [Single protein] structure of sequence from [Archaeoglobus fulgidus] with APR as [ligand]. Structure known Active Site: AC1. 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

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