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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biochemical function
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heat shock protein binding
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1 term
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DOI no:
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EMBO J
20:295-304
(2001)
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PubMed id:
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Structural basis for the inactivation of retinoblastoma tumor suppressor by SV40 large T antigen.
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H.Y.Kim,
B.Y.Ahn,
Y.Cho.
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ABSTRACT
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Inactivation of the retinoblastoma (Rb) tumor suppressor by Simian virus 40
(SV40) large T antigen is one of the central features of tumorigenesis induced
by SV40. Both the N-terminal J domain and the LxCxE motif of large T antigen are
required for inactivation of Rb. The crystal structure of the N-terminal region
(residues 7-117) of SV40 large T antigen bound to the pocket domain of Rb
reveals that large T antigen contains a four-helix bundle, and residues from
helices alpha2 and alpha4 and from a loop containing the LxCxE motif participate
in the interactions with Rb. The two central helices and a connecting loop in
large T antigen have structural similarities with the J domains of the molecular
chaperones DnaJ and HDJ-1, suggesting that large T antigen may use a chaperone
mechanism for its biological function. However, there are significant
differences between large T antigen and the molecular chaperones in other
regions and these differences are likely to provide the specificity needed for
large T antigen to inactivate Rb.
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Selected figure(s)
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Figure 2.
Figure 2 (A) Overall structure of the N-terminal portion of SV40
large T antigen (residues 7 -117). The two central helices and
connecting loop are colored red, surrounding helices are in
green and the other loops are colored gray. (B) Sequence
alignment of T antigen with other J domain-containing proteins.
The conserved residues are boxed with yellow and green. Residues
participating in core formation (side chains with <20% of
accessible surface area) are indicated by red circles and those
interacting with Rb by blue triangles. JCV, large T antigen of
JC virus; BKV, large T antigen of BK virus; PyV, large T antigen
of murine polyoma virus. The conserved residues in HPV E7 and
adenovirus E1 are boxed in red lines. (C) Structural comparison
of SV40 large T antigen (yellow) with the J domain of DnaJ
(blue) and HDJ-1 (red). Helix 4'
is from DnaJ or HDJ-1, and helix 4
is from large T antigen. (D) Stereo view of the hydrophobic core
structure of large T antigen. Helix 1
is colored green, 2
and 3
magenta, and 4
light blue. (E) The local structure of the L2 loop of large T
antigen. The side chain of Phe41 is stacked between Trp91
(green) in helix 4
and Pro43.
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Figure 5.
Figure 5 (A) Schematic representation of the dissociation
mechanism of the Rb -E2F complex by large T antigen and hsc70.
The model is based on the DnaJ -DnaK chaperone mechanism
proposed by Laufen et al. (1999); see text. (B) Surface
representation of a model for the interaction between the Rb
pocket domain -large T antigen complex and hsc70 (DnaK).
Residues Arg167, Asn170 and Thr173 are critical for the
interaction with the J domain, whereas Asn147, Asp148 and Glu152
do not a play significant role in binding to the J domain (Suh
et al., 1998). The model is based on information from NMR
perturbation and mutational analysis of the DnaJ -DnaK
interaction (see text). The solvent-accessible surface was
calculated using GRASP (Nicholls et al., 1991) with a water
probe radius of 1.4 Å, and is colored by electrostatic potential
of large T antigen and hsc70 in the range less than -10 to >10
K[b]T, where K[b] is the Boltzman constant and T is the
temperature. The positive potential is shown in blue and
negative in red.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2001,
20,
295-304)
copyright 2001.
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Figures were
selected
by the author.
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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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PDB code:
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B.Xiao,
J.Spencer,
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| |
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PDB code:
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D.W.Goodrich
(2003).
How the other half lives, the amino-terminal domain of the retinoblastoma tumor suppressor protein.
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J Cell Physiol, 197,
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K.Munger
(2003).
Clefts, grooves, and (small) pockets: the structure of the retinoblastoma tumor suppressor in complex with its cellular target E2F unveiled.
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| |
Proc Natl Acad Sci U S A, 100,
2165-2167.
|
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M.G.Gomez-Lorenzo,
M.Valle,
J.Frank,
C.Gruss,
C.O.Sorzano,
X.S.Chen,
L.E.Donate,
and
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(2003).
Large T antigen on the simian virus 40 origin of replication: a 3D snapshot prior to DNA replication.
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| |
EMBO J, 22,
6205-6213.
|
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P.Genevaux,
F.Lang,
F.Schwager,
J.V.Vartikar,
K.Rundell,
J.M.Pipas,
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Simian virus 40 T antigens and J domains: analysis of Hsp40 cochaperone functions in Escherichia coli.
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| |
J Virol, 77,
10706-10713.
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R.Roy,
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The cap region of topoisomerase I binds to sites near both ends of simian virus 40 T antigen.
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| |
J Virol, 77,
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|
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S.J.Landry
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|
| |
Biochemistry, 42,
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Y.Kudinov,
C.L.Wiseman,
and
A.I.Kharazi
(2003).
Phorbol myristate acetate and Bryostatin 1 rescue IFN-gamma inducibility of MHC class II molecules in LS1034 colorectal carcinoma cell line.
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Cancer Cell Int, 3,
4.
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C.Lee,
J.H.Chang,
H.S.Lee,
and
Y.Cho
(2002).
Structural basis for the recognition of the E2F transactivation domain by the retinoblastoma tumor suppressor.
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Genes Dev, 16,
3199-3212.
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PDB code:
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C.Lee,
and
Y.Cho
(2002).
Interactions of SV40 large T antigen and other viral proteins with retinoblastoma tumour suppressor.
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Rev Med Virol, 12,
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C.S.Sullivan,
and
J.M.Pipas
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T antigens of simian virus 40: molecular chaperones for viral replication and tumorigenesis.
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Microbiol Mol Biol Rev, 66,
179-202.
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F.A.Dick,
and
N.J.Dyson
(2002).
Three regions of the pRB pocket domain affect its inactivation by human papillomavirus E7 proteins.
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| |
J Virol, 76,
6224-6234.
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P.Genevaux,
F.Schwager,
C.Georgopoulos,
and
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(2002).
Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain.
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Genetics, 162,
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P.T.Reilly,
J.Wysocka,
and
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Inactivation of the retinoblastoma protein family can bypass the HCF-1 defect in tsBN67 cell proliferation and cytokinesis.
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Mol Cell Biol, 22,
6767-6778.
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S.W.Fewell,
D.M.Markle,
and
J.L.Brodsky
(2002).
The carboxy terminus of simian virus 40 large T antigen is required to disrupt the yeast cell cycle.
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J Virol, 76,
4621-4624.
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S.W.Fewell,
J.M.Pipas,
and
J.L.Brodsky
(2002).
Mutagenesis of a functional chimeric gene in yeast identifies mutations in the simian virus 40 large T antigen J domain.
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Proc Natl Acad Sci U S A, 99,
2002-2007.
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V.D.Brown,
and
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(2002).
The B-domain lysine patch of pRB is required for binding to large T antigen and release of E2F by phosphorylation.
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Mol Cell Biol, 22,
1390-1401.
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S.W.Fewell,
K.J.Travers,
J.S.Weissman,
and
J.L.Brodsky
(2001).
The action of molecular chaperones in the early secretory pathway.
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Annu Rev Genet, 35,
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Where a reference describes a PDB structure, the PDB
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shown on the right.
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