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PDBsum entry 2l84
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Solution nmr structures of cbp bromodomain with small molecule j28
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Structure:
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Creb-binding protein. Chain: a. Fragment: bromo domain residues 1081-1197. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: crebbp, cbp. Expressed in: escherichia coli. Expression_system_taxid: 526563.
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NMR struc:
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20 models
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Authors:
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J.C.Borah,S.Mujtaba,I.Karakikes,L.Zeng,M.Muller,J.Patel,N.Moshkina, K.Morohashi,W.Zhang,G.Gerona-Navarro,R.J.Hajjar,M.Zhou
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Key ref:
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J.C.Borah
et al.
(2011).
A small molecule binding to the coactivator CREB-binding protein blocks apoptosis in cardiomyocytes.
Chem Biol,
18,
531-541.
PubMed id:
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Date:
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03-Jan-11
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Release date:
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19-Jan-11
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PROCHECK
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Headers
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References
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Q92793
(CBP_HUMAN) -
CREB-binding protein from Homo sapiens
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Seq: Struc:
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2442 a.a.
121 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Enzyme class 1:
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E.C.2.3.1.-
- ?????
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Enzyme class 2:
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E.C.2.3.1.48
- histone acetyltransferase.
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Reaction:
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L-lysyl-[protein] + acetyl-CoA = N6-acetyl-L-lysyl-[protein] + CoA + H+
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L-lysyl-[protein]
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acetyl-CoA
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=
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N(6)-acetyl-L-lysyl-[protein]
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+
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CoA
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+
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H(+)
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Chem Biol
18:531-541
(2011)
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PubMed id:
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A small molecule binding to the coactivator CREB-binding protein blocks apoptosis in cardiomyocytes.
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J.C.Borah,
S.Mujtaba,
I.Karakikes,
L.Zeng,
M.Muller,
J.Patel,
N.Moshkina,
K.Morohashi,
W.Zhang,
G.Gerona-Navarro,
R.J.Hajjar,
M.M.Zhou.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.H.Arrowsmith,
C.Bountra,
P.V.Fish,
K.Lee,
and
M.Schapira
(2012).
Epigenetic protein families: a new frontier for drug discovery.
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Nat Rev Drug Discov,
11,
384-400.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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