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PDBsum entry 1a5j
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DNA binding protein
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PDB id
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1a5j
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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DNA binding protein
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Title:
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Chicken b-myb DNA binding domain, repeat 2 and repeat3, nmr, 32 structures
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Structure:
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B-myb. Chain: a. Fragment: DNA binding domain, repeat 2 and repeat 3. Engineered: yes
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Source:
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Gallus gallus. Chicken. Organism_taxid: 9031. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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32 models
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Authors:
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P.B.Mcintosh,M.D.Carr,U.Wollborn,T.A.Frenkiel,J.Feeney,J.E.Mccormick, K.H.Klempnauer
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Key ref:
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P.B.McIntosh
et al.
(1998).
Solution structure of the B-Myb DNA-binding domain: a possible role for conformational instability of the protein in DNA binding and control of gene expression.
Biochemistry,
37,
9619-9629.
PubMed id:
DOI:
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Date:
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16-Feb-98
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Release date:
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01-Jul-98
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PROCHECK
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Headers
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References
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Q03237
(MYBB_CHICK) -
Myb-related protein B from Gallus gallus
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Seq:
Struc:
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686 a.a.
110 a.a.*
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Key: |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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Biochemistry
37:9619-9629
(1998)
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PubMed id:
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Solution structure of the B-Myb DNA-binding domain: a possible role for conformational instability of the protein in DNA binding and control of gene expression.
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P.B.McIntosh,
T.A.Frenkiel,
U.Wollborn,
J.E.McCormick,
K.H.Klempnauer,
J.Feeney,
M.D.Carr.
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ABSTRACT
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Double- and triple-resonance heteronuclear NMR spectroscopy have been used to
determine the high-resolution solution structure of the minimal B-Myb
DNA-binding domain (B-MybR2R3) and to characterize the specific complex formed
with a synthetic DNA fragment corresponding to the Myb target site on the
Myb-regulated gene tom-1. B-MybR2R3 is shown to consist of two independent
protein domains (R2 and R3) joined by a short linker, which have strikingly
different tertiary structures despite significant sequence similarities. In
addition, the C-terminal region of B-Myb R2 is confirmed to have a poorly
defined structure, reflecting the existence of multiple conformations in slow to
intermediate exchange. This contrasts with the tertiary structure reported for
c-MybR2R3, in which both R2 and R3 have the same fold and the C-terminal region
of R2 forms a stable, well-defined helix [Ogata, K., et al. (1995) Nat. Struct.
Biol. 2, 309-320]. The NMR data suggest there are extensive contacts between
B-MybR2R3 and its DNA target site in the complex and are consistent with a
significant conformational change in the protein on binding to DNA, with one
possibility being the formation of a stable helix in the C-terminal region of
R2. In addition, conformational heterogeneity identified in R2 of B-MybR2R3
bound to the tom-1-A target site may play an important role in the control of
gene expression by Myb proteins.
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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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G.Lang,
W.M.Gombert,
and
H.J.Gould
(2005).
A transcriptional regulatory element in the coding sequence of the human Bcl-2 gene.
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Immunology,
114,
25-36.
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M.D.Carr,
M.J.Bloemink,
E.Dentten,
A.O.Whelan,
S.V.Gordon,
G.Kelly,
T.A.Frenkiel,
R.G.Hewinson,
and
R.A.Williamson
(2003).
Solution structure of the Mycobacterium tuberculosis complex protein MPB70: from tuberculosis pathogenesis to inherited human corneal desease.
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J Biol Chem,
278,
43736-43743.
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PDB code:
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L.R.Johnson,
T.K.Johnson,
M.Desler,
T.A.Luster,
T.Nowling,
R.E.Lewis,
and
A.Rizzino
(2002).
Effects of B-Myb on gene transcription: phosphorylation-dependent activity ans acetylation by p300.
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J Biol Chem,
277,
4088-4097.
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S.Bergholtz,
T.O.Andersen,
K.B.Andersson,
J.Borrebaek,
B.Lüscher,
and
O.S.Gabrielsen
(2001).
The highly conserved DNA-binding domains of A-, B- and c-Myb differ with respect to DNA-binding, phosphorylation and redox properties.
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Nucleic Acids Res,
29,
3546-3556.
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O.V.Galzitskaya,
A.K.Surin,
and
H.Nakamura
(2000).
Optimal region of average side-chain entropy for fast protein folding.
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Protein Sci,
9,
580-586.
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A.Sala,
and
R.Watson
(1999).
B-Myb protein in cellular proliferation, transcription control, and cancer: latest developments.
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J Cell Physiol,
179,
245-250.
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K.B.Andersson,
T.Berge,
V.Matre,
and
O.S.Gabrielsen
(1999).
Sequence selectivity of c-Myb in vivo. Resolution of a DNA target specificity paradox.
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J Biol Chem,
274,
21986-21994.
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R.A.Williamson,
F.W.Muskett,
M.J.Howard,
R.B.Freedman,
and
M.D.Carr
(1999).
The effect of matrix metalloproteinase complex formation on the conformational mobility of tissue inhibitor of metalloproteinases-2 (TIMP-2).
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J Biol Chem,
274,
37226-37232.
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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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
