2bfq
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The ADP-ribosylation of proteins is an important post-translational | + | 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== | ==About this Structure== | ||
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[[Category: Archaeoglobus fulgidus]] | [[Category: Archaeoglobus fulgidus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Allen, M | + | [[Category: Allen, M D.]] |
| - | [[Category: Buhecha, H | + | [[Category: Buhecha, H R.]] |
[[Category: Bycroft, M.]] | [[Category: Bycroft, M.]] | ||
| - | [[Category: Karras, G | + | [[Category: Karras, G I.]] |
| - | [[Category: Ladurner, A | + | [[Category: Ladurner, A G.]] |
[[Category: Pugieux, C.]] | [[Category: Pugieux, C.]] | ||
[[Category: Sait, F.]] | [[Category: Sait, F.]] | ||
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[[Category: nucleotide]] | [[Category: nucleotide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:20 2008'' |
Revision as of 14:37, 21 February 2008
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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 with as ligand. 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
Page seeded by OCA on Thu Feb 21 16:37:20 2008
