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PDBsum entry 2fk4
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Metal binding protein, oncoprotein
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PDB id
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2fk4
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References listed in PDB file
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Key reference
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Title
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Structural and functional analysis of e6 oncoprotein: insights in the molecular pathways of human papillomavirus-Mediated pathogenesis.
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Authors
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Y.Nominé,
M.Masson,
S.Charbonnier,
K.Zanier,
T.Ristriani,
F.Deryckère,
A.P.Sibler,
D.Desplancq,
R.A.Atkinson,
E.Weiss,
G.Orfanoudakis,
B.Kieffer,
G.Travé.
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Ref.
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Mol Cell, 2006,
21,
665-678.
[DOI no: ]
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PubMed id
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Abstract
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Oncoprotein E6 is essential for oncogenesis induced by human papillomaviruses
(HPVs). The solution structure of HPV16-E6 C-terminal domain reveals a zinc
binding fold. A model of full-length E6 is proposed and analyzed in the context
of HPV evolution. E6 appears as a chameleon protein combining a conserved
structural scaffold with highly variable surfaces participating in generic or
specialized HPV functions. We investigated surface residues involved in two
specialized activities of high-risk genital HPV E6: p53 tumor suppressor
degradation and nucleic acid binding. Screening of E6 surface mutants identified
an in vivo p53 degradation-defective mutant that fails to recruit p53 to
ubiquitin ligase E6AP and restores high p53 levels in cervical carcinoma cells
by competing with endogeneous E6. We also mapped the nucleic acid binding
surface of E6, the positive potential of which correlates with genital
oncogenicity. E6 structure-function analysis provides new clues for
understanding and counteracting the complex pathways of HPV-mediated
pathogenesis.
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Figure 1.
Figure 1. Solution Structure of E6C
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Figure 4.
Figure 4. Examples of Residue Specialization in HPV Species
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2006,
21,
665-678)
copyright 2006.
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Secondary reference #1
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Title
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1h and 15n resonance assignment, Secondary structure and dynamic behaviour of the c-Terminal domain of human papillomavirus oncoprotein e6.
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Authors
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Y.Nominé,
S.Charbonnier,
L.Miguet,
N.Potier,
A.Van dorsselaer,
R.A.Atkinson,
G.Travé,
B.Kieffer.
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Ref.
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J Biomol Nmr, 2005,
31,
129-141.
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PubMed id
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