Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2005-6-1
pubmed:databankReference
pubmed:abstractText
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.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-10365964, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-10372352, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-10455009, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-10471322, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-10494847, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-10550052, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-10607829, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-10744766, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-10827952, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-11016934, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-11080160, http://linkedlifedata.com/resource/pubmed/commentcorrection/15902274-11110709, 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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate Ribose, http://linkedlifedata.com/resource/pubmed/chemical/Archaeal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/BAL protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histones, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Poa1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Poly Adenosine Diphosphate Ribose, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0261-4189
pubmed:author
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