Modeling and Molecular Dynamics of the 3D Structure of the HPV16 E7 Protein and Its Variants
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 pro...
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| Veröffentlicht in: | International journal of molecular sciences 2021-01, Vol.22 (3), p.1400 |
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| creator | Bello-Rios, Ciresthel Montaño, Sarita Garibay-Cerdenares, Olga Lilia Araujo-Arcos, Lilian Esmeralda Leyva-Vázquez, Marco Antonio Illades-Aguiar, Berenice |
| description | 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. |
| doi_str_mv | 10.3390/ijms22031400 |
| format | Article |
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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.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms22031400</identifier><identifier>PMID: 33573298</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino acid sequence ; Amino acids ; Cell cycle ; Cervical cancer ; Cervix ; E7 protein ; Epidemiology ; Homology ; Human papillomavirus ; Kinases ; Modelling ; Molecular dynamics ; Molecular structure ; Mutation ; Phosphorylation ; Protein structure ; Proteins ; Simulation ; Uncertainty analysis</subject><ispartof>International journal of molecular sciences, 2021-01, Vol.22 (3), p.1400</ispartof><rights>2021. 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| subjects | Amino acid sequence Amino acids Cell cycle Cervical cancer Cervix E7 protein Epidemiology Homology Human papillomavirus Kinases Modelling Molecular dynamics Molecular structure Mutation Phosphorylation Protein structure Proteins Simulation Uncertainty analysis |
| title | Modeling and Molecular Dynamics of the 3D Structure of the HPV16 E7 Protein and Its Variants |
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