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PDBsum entry 1gv5
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Transcription
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PDB id
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1gv5
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of c-Myb DNA-Binding domain: specific na+ binding and correlation with nmr structure
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Authors
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T.H.Tahirov,
H.Morii,
H.Uedaira,
M.Sasaki,
A.Sarai,
S.Adachi,
S.Y.Park,
N.Kamiya,
K.Ogata.
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Ref.
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To be Published ...
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Secondary reference #1
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Title
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Mechanism of c-Myb-C/ebp beta cooperation from separated sites on a promoter.
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Authors
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T.H.Tahirov,
K.Sato,
E.Ichikawa-Iwata,
M.Sasaki,
T.Inoue-Bungo,
M.Shiina,
K.Kimura,
S.Takata,
A.Fujikawa,
H.Morii,
T.Kumasaka,
M.Yamamoto,
S.Ishii,
K.Ogata.
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Ref.
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Cell, 2002,
108,
57-70.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2. DNA Recognition by c-Myb and AMV v-Myb(A and B)
Schematic representations of DNA recognition by c-Myb (A) and
AMV v-Myb (B). Dashed and solid lines depict intermolecular
hydrogen bonds and van der Waals contacts, respectively. DNA
bases labeled in red are involved in direct interactions with
proteins.(C) Stereo view of specific interactions between c-Myb
and DNA bases. The peptide backbone of c-Myb is drawn as a pink
or blue tube in the R2 and R3 regions, respectively. Thin and
bold dotted lines depict intermolecular hydrogen bonds and van
der Waals interactions, respectively. Water molecules are shown
as red balls.(D and E) Electrostatic surface potential of
DNA-bound c-Myb R1R2R3 viewed from the front (D) and back (E);
positively and negatively charged areas are colored blue and
red, respectively.
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Figure 3.
Figure 3. Structural Differences between c-Myb R2 and AMV
v-Myb R2 and Close-Up Views of the Interactions among c-Myb,
C/EBPβ, and DNA(A) Stereo view of the superimposed R2 domains
within c-Myb (pink) and AMV v-Myb (gray) complexes. The peptide
backbones are drawn as tubes, and the side chains of residues
that are mutated or exhibit different conformations in AMV v-Myb
are drawn as sticks.(B) A close-up view of the interactions
between the Arg114 and Trp115 backbones and the DNA phosphate
oxygens at G4′ within the c-Myb and AMV v-Myb complexes.(C)
Stereo view of the c-Myb–C/EBPβ interaction site.
Intermolecular hydrogen bonds and K^+-mediated interactions are
represented by dotted lines. Parts of c-Myb and C/EBPβ chains A
and B are drawn as pink, yellow, and green sticks, respectively.
The part of the DNA backbone interacting with the C/EBPβ
leucine zipper region is also shown. The metal binding sites of
R1, R2, and R3 were confirmed by their high-resolution crystal
structures (T.T. et al., submitted).(D) Summary of the
intermolecular van der Waals interactions between c-Myb and
C/EBPβ.(E) Stereo view of the c-Myb–C/EBPβ-DNA interaction
site highlighting the interactions involved in stabilization of
the α1–α2 loop of c-Myb R2. The peptide backbones of
DNA-bound c-Myb (pink) and C/EBPβ chains A (yellow) and B
(green) are drawn as tubes. Free c-Myb R2 (blue) is superimposed
on the DNA-bound c-Myb R2. An alternative position for the
disordered portion of the α1–α2 loop of the free c-Myb R2 is
colored dark blue.
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The above figures are
reproduced from the cited reference
with permission from Cell Press
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Secondary reference #2
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Title
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Crystallization and preliminary X-Ray analysis of wild-Type and V103l mutant myb r2 DNA-Binding domain.
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Authors
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T.H.Tahirov,
H.Morii,
H.Uedaira,
A.Sarai,
K.Ogata.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1999,
55,
1345-1347.
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PubMed id
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