2bfq: Difference between revisions

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{{STRUCTURE_2bfq|  PDB=2bfq  |  SCENE=  }}  
{{STRUCTURE_2bfq|  PDB=2bfq  |  SCENE=  }}  


'''MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES'''
===MACRO DOMAINS ARE ADP-RIBOSE BINDING MOLECULES===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15902274}}


==About this Structure==
==About this Structure==
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[[Category: Macro_h2a domain/hydrolase]]
[[Category: Macro_h2a domain/hydrolase]]
[[Category: Nucleotide]]
[[Category: Nucleotide]]
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