2bfq: Difference between revisions
New page: left|200px<br /> <applet load="2bfq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bfq, resolution 1.5Å" /> '''MACRO DOMAINS ARE AD... |
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==About this Structure== | ==About this Structure== | ||
2BFQ 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 APR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BFQ OCA]]. | 2BFQ 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 APR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BFQ OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: nucleotide]] | [[Category: nucleotide]] | ||
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Revision as of 13:40, 30 October 2007
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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] with APR as [ligand]. Structure known Active Site: AC1. 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
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