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2bfr

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(New page: 200px<br /> <applet load="2bfr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bfr, resolution 2.5&Aring;" /> '''THE MACRO DOMAIN IS ...)
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Revision as of 17:38, 29 October 2007

Image:2bfr.gif

2bfr, resolution 2.5Å

Drag the structure with the mouse to rotate

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 MG and ADP as [ligands]. 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 Oct 29 19:42:46 2007

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