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PDBsum entry 1dc2
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Gene regulation
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PDB id
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1dc2
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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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Tumor suppressor ink4: refinement of p16ink4a structure and determination of p15ink4b structure by comparative modeling and nmr data.
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Authors
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C.Yuan,
T.L.Selby,
J.Li,
I.J.Byeon,
M.D.Tsai.
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Ref.
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Protein Sci, 2000,
9,
1120-1128.
[DOI no: ]
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PubMed id
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Abstract
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Within the tumor suppressor protein INK4 (inhibitor of cyclin-dependent kinase
4) family, p15INK4B is the smallest and the only one whose structure has not
been determined previously, probably due to the protein's conformational
flexibility and instability. In this work, multidimensional NMR studies were
performed on this protein. The first tertiary structure was built by comparative
modeling with p16INK4A as the template, followed by restrained energy
minimization with NMR constraints (NOE and H-bonds). For this purpose, the
solution structure of pl6INK4A, whose quality was also limited by similar
problems, was refined with additional NMR experiments conducted on an 800 MHz
spectrometer and by structure-based iterative NOE assignments. The nonhelical
regions showed major improvement with root-mean-square deviation (RMSD) improved
from 1.23 to 0.68 A for backbone heavy atoms. The completion of p15INK4B coupled
with refinement of p16INK4A made it possible to compare the structures of the
four INK4 members in depth, and to compare the structures of p16INK4A in the
free form and in the p16INK4A-CDK6 complex. This is an important step toward a
comprehensive understanding of the precise functional roles of each INK4 member.
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Secondary reference #1
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Title
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Tumor suppressor p16ink4a: determination of solution structure and analyses of its interaction with cyclin-Dependent kinase 4.
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Authors
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I.J.Byeon,
J.Li,
K.Ericson,
T.L.Selby,
A.Tevelev,
H.J.Kim,
P.O'Maille,
M.D.Tsai.
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Ref.
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Mol Cell, 1998,
1,
421-431.
[DOI no: ]
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PubMed id
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Figure 4.
Figure 4. Assay of p16 ActivityGels of in vitro
phosphorylation of pRb by cdk4 in the presence of increasing
concentrations of wild-type p16 (A) and D84H (B). Lanes 1 and 2
are negative controls.
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Figure 7.
Figure 7. Working Model for the C5–p16 ComplexThe model
is depicted such that the ionic interactions between specific
charged residues are visible. Side chains of Arg-24 and Glu-7 of
C5 (blue ribbon) are shown in ball-and-stick mode. The p16
residue facing C5/Arg-24 is Glu-69, and that facing C5/Glu-7 is
Arg-47. C5/Lys-22 could interact with p16/Asp-74. The p16
structure shown is 140° rotated from that in Figure 3B.
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The above figures are
reproduced from the cited reference
with permission from Cell Press
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