Ordered self-assembly mechanism of a spherical oncoprotein oligomer triggered by zinc removal and stabilized by an intrinsically disordered domain

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Background: Self-assembly is a common theme in proteins of unrelated sequences or functions. The human papillomavirus E7 oncoprotein is an extended dimer with an intrinsically disordered domain, that can form large spherical oligomers. These are the major species in the cytosol of HPV transformed an...

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Detalles Bibliográficos
Autores principales: Smal, C., Alonso, L.G., Wetzler, D.E., Heer, A., de Prat Gay, G.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 2012
Materias:
amyloid precursor protein
amyloid protein
chaperone
oligomer
protein E7
zinc
oncogene protein E7, Human papillomavirus type 16
amino terminal sequence
article
carboxy terminal sequence
circular dichroism
concentration (parameters)
drug research
immunogenicity
kinetics
nanotechnology
oligomerization
protein assembly
protein binding
protein conformation
protein domain
protein polymerization
protein quaternary structure
protein secondary structure
protein stability
protein tertiary structure
Wart virus
chemistry
genetics
human
Human papillomavirus type 16
metabolism
protein multimerization
Human papillomavirus
Human papillomavirus 16
Humans
Papillomavirus E7 Proteins
Protein Multimerization
Protein Stability
Protein Structure, Quaternary
Protein Structure, Tertiary
Zinc
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_19326203_v7_n5_p_Smal
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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