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Modeling and Molecular Dynamics of the 3D Structure of the HPV16 E7 Protein and Its Variants.
Bello-Rios, Ciresthel; Montaño, Sarita; Garibay-Cerdenares, Olga Lilia; Araujo-Arcos, Lilian Esmeralda; Leyva-Vázquez, Marco Antonio; Illades-Aguiar, Berenice.
Afiliación
  • Bello-Rios C; Laboratorio de Biomedicina Molecular, Facultad de Ciencias Químico-Biológicas, Universidad Autonóma de Guerrero, Chilpancingo, CP 39087, Mexico.
  • Montaño S; Laboratorio de Bioinformática y Simulación Molecular, Facultad de Ciencias Químico Biológicas, Universidad Autónoma de Sinaloa, Culiacán Sinaloa, CP 80030, Mexico.
  • Garibay-Cerdenares OL; Laboratorio de Biomedicina Molecular, Facultad de Ciencias Químico-Biológicas, Universidad Autonóma de Guerrero, Chilpancingo, CP 39087, Mexico.
  • Araujo-Arcos LE; CONACyT-Universdad Autónoma de Guerrero, Chilpancingo, CP 39087, Mexico.
  • Leyva-Vázquez MA; Laboratorio de Biomedicina Molecular, Facultad de Ciencias Químico-Biológicas, Universidad Autonóma de Guerrero, Chilpancingo, CP 39087, Mexico.
  • Illades-Aguiar B; Laboratorio de Biomedicina Molecular, Facultad de Ciencias Químico-Biológicas, Universidad Autonóma de Guerrero, Chilpancingo, CP 39087, Mexico.
Int J Mol Sci ; 22(3)2021 Jan 30.
Article en En | MEDLINE | ID: mdl-33573298
The oncogenic potential of high-risk human papillomavirus (HPV) is predicated on the production of the E6 and E7 oncoproteins, which are responsible for disrupting the control of the cell cycle. Epidemiological studies have proposed that the presence of the N29S and H51N variants of the HPV16 E7 protein is significantly associated with cervical cancer. It has been suggested that changes in the amino acid sequence of E7 variants may affect the oncoprotein 3D structure; however, this remains uncertain. An analysis of the structural differences of the HPV16 E7 protein and its variants (N29S and H51N) was performed through homology modeling and structural refinement by molecular dynamics simulation. We propose, for the first time, a 3D structure of the E7 reference protein and two of Its variants (N29S and H51N), and conclude that the mutations induced by the variants in N29S and H51N have a significant influence on the 3D structure of the E7 protein of HPV16, which could be related to the oncogenic capacity of this protein.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Papillomavirus Humano 16 / Proteínas E7 de Papillomavirus Límite: Female / Humans Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: México Pais de publicación: Suiza
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Papillomavirus Humano 16 / Proteínas E7 de Papillomavirus Límite: Female / Humans Idioma: En Revista: Int J Mol Sci Año: 2021 Tipo del documento: Article País de afiliación: México Pais de publicación: Suiza