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2bfr

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Revision as of 14:37, 21 February 2008 by OCA (Talk | contribs)
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Image:2bfr.jpg

2bfr, resolution 2.5Å

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THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE

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

2BFR is a Single protein structure of sequence from Archaeoglobus fulgidus with and as ligands. Known structural/functional Site: . 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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