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2bfr
From Proteopedia
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| - | [[Image:2bfr.jpg|left|200px]]<br /><applet load="2bfr" size=" | + | [[Image:2bfr.jpg|left|200px]]<br /><applet load="2bfr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bfr, resolution 2.5Å" /> | caption="2bfr, resolution 2.5Å" /> | ||
'''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== | ||
| - | 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:// | + | 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 <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nucleotide]] | [[Category: nucleotide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:23:35 2008'' |
Revision as of 08:23, 3 February 2008
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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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