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PDBsum entry 2f8b
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Oncoprotein, virus/viral protein
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PDB id
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2f8b
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References listed in PDB file
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Key reference
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Title
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Solution structure of the partially folded high-Risk human papilloma virus 45 oncoprotein e7.
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Authors
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O.Ohlenschläger,
T.Seiboth,
H.Zengerling,
L.Briese,
A.Marchanka,
R.Ramachandran,
M.Baum,
M.Korbas,
W.Meyer-Klaucke,
M.Dürst,
M.Görlach.
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Ref.
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Oncogene, 2006,
25,
5953-5959.
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PubMed id
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Abstract
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The oncoprotein E7 of human papilloma viruses (HPV) is involved in the
pathogenesis and maintenance of human cervical cancers. The most prevalent HPV
types found in cervix carcinomas are HPV16, 18 and 45. The structure of the E7
dimer from HPV45 (PDB 2F8B) was determined by nuclear magnetic resonance
spectroscopy. Each monomer comprises an unfolded N-terminus and a
well-structured C-terminal domain with a beta1beta2alpha1beta3alpha2 topology
representing a unique zinc-binding fold found only for E7. Dimerization occurs
through the alpha1/alpha1' helices and intermolecular beta-sheet formation but
excludes the zinc-binding sites. E7 is reported to interact with a number of
cellular proteins (e.g. pRb, p21(CIP1)). Binding of a peptide derived from the
C-terminus of p21(CIP1) to the C-terminal domain of E7 was characterized by
monitoring chemical shift perturbations of the amide groups of E7. This provides
direct evidence that a shallow groove situated between alpha1 and beta1 of the
E7 C-terminal domain is interacting with the C-terminus of p21(CIP1).
Intriguingly, this binding site overlaps with the low-affinity binding site on
E7 for the C-domain of pRb.
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