2bfq: Difference between revisions
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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.]] | ||
[[Category: | [[Category: Crystal structure p-loop]] | ||
[[Category: | [[Category: Histone macroh2a]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Macro_h2a domain/hydrolase]] | ||
[[Category: | [[Category: Nucleotide]] | ||
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Revision as of 20:13, 3 May 2008
MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES
OverviewOverview
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 StructureAbout this Structure
2BFQ is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
ReferenceReference
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