High-risk (HPV16) human papillomavirus E7 oncoprotein is highly stable and extended, with conformational transitions that could explain its multiple cellular binding partners

High-risk papillomaviruses are known to exert their transforming activity mainly through E7, one of their two oncoproteins. Despite its relevance, no structural information has been obtained that could explain the apparent broad binding specificity of E7. Recombinant E7 from HPV-16 purified to near...

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Detalles Bibliográficos
Autores principales: Alonso, L.G., García-Alai, M.M., Nadra, A.D., Lapeña, A.N., Almeida, F.L., Gualfetti, P., De Prat-Gay, G.
Formato: JOUR
Materias:
Hydrophobic surfaces
Conformations
Dimers
Hydrodynamics
Light scattering
Molecular weight
Proteins
Biochemistry
oncoprotein
article
binding affinity
circular dichroism
conformational transition
gel filtration chromatography
hydrodynamics
light scattering
molecular weight
nonhuman
priority journal
protein binding
protein conformation
protein denaturation
protein protein interaction
protein purification
protein stability
protein structure
spectral sensitivity
structure analysis
Wart virus
Anilino Naphthalenesulfonates
Cell Transformation, Viral
Circular Dichroism
Dimerization
Electrophoresis, Polyacrylamide Gel
Guanidine
Heat
Humans
Hydrogen-Ion Concentration
Hydrophobicity
Oncogene Proteins, Viral
Papillomaviridae
Protein Binding
Protein Conformation
Protein Denaturation
Protein Folding
Risk Factors
Sodium Dodecyl Sulfate
Solvents
DNA viruses
Human papillomavirus
Human papillomavirus type 16
Human papillomavirus types
Papillomavirus
Papovaviridae
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00062960_v41_n33_p10510_Alonso
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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