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2bfq

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[[Image:2bfq.gif|left|200px]]
[[Image:2bfq.gif|left|200px]]
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{{Structure
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|PDB= 2bfq |SIZE=350|CAPTION= <scene name='initialview01'>2bfq</scene>, resolution 1.5&Aring;
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The line below this paragraph, containing "STRUCTURE_2bfq", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Apr+Binding+Site+For+Chain+A'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>
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|ACTIVITY=
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{{STRUCTURE_2bfq| PDB=2bfq | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfq OCA], [http://www.ebi.ac.uk/pdbsum/2bfq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bfq RCSB]</span>
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'''MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES'''
'''MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES'''
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[[Category: Pugieux, C.]]
[[Category: Pugieux, C.]]
[[Category: Sait, F.]]
[[Category: Sait, F.]]
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[[Category: crystal structure p-loop]]
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[[Category: Crystal structure p-loop]]
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[[Category: histone macroh2a]]
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[[Category: Histone macroh2a]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: macro_h2a domain/hydrolase]]
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[[Category: Macro_h2a domain/hydrolase]]
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[[Category: nucleotide]]
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[[Category: Nucleotide]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:13:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:05:44 2008''
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Revision as of 17:13, 3 May 2008

Image:2bfq.gif

Template:STRUCTURE 2bfq

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. 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 Sat May 3 20:13:46 2008

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