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2bfq
From Proteopedia
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| - | [[Image:2bfq.gif|left|200px]] | + | [[Image:2bfq.gif|left|200px]] |
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| - | '''MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES''' | + | {{Structure |
| + | |PDB= 2bfq |SIZE=350|CAPTION= <scene name='initialview01'>2bfq</scene>, resolution 1.5Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Apr+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BFQ is a [ | + | 2BFQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFQ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15902274 15902274] |
[[Category: Archaeoglobus fulgidus]] | [[Category: Archaeoglobus fulgidus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: nucleotide]] | [[Category: nucleotide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:01:21 2008'' |
Revision as of 14:01, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 16:01:21 2008
