2bfr

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[[Image:2bfr.gif|left|200px]]<br />
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[[Image:2bfr.jpg|left|200px]]<br /><applet load="2bfr" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="2bfr" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2bfr, resolution 2.5&Aring;" />
caption="2bfr, resolution 2.5&Aring;" />
'''THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE'''<br />
'''THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE'''<br />
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==About this Structure==
==About this Structure==
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2BFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BFR OCA].
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2BFR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Adp Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BFR OCA].
==Reference==
==Reference==
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[[Category: nucleotide]]
[[Category: nucleotide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:37:01 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:45:29 2007''

Revision as of 16:35, 18 December 2007


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 MG and ADP 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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