Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Modeling and Molecular Dynamics of the 3D Structure of the HPV16 E7 Protein and Its Variants

Version 1 : Received: 24 December 2020 / Approved: 25 December 2020 / Online: 25 December 2020 (16:05:04 CET)

How to cite: Bello-Rios, C.; Montaño, S.; Garibay-Cerdenares, O.L.; Araujo-Arcos, L.E.; Leyva-Vázquez, M.A.; Illades-Aguiar, B. Modeling and Molecular Dynamics of the 3D Structure of the HPV16 E7 Protein and Its Variants. Preprints 2020, 2020120671 (doi: 10.20944/preprints202012.0671.v1). Bello-Rios, C.; Montaño, S.; Garibay-Cerdenares, O.L.; Araujo-Arcos, L.E.; Leyva-Vázquez, M.A.; Illades-Aguiar, B. Modeling and Molecular Dynamics of the 3D Structure of the HPV16 E7 Protein and Its Variants. Preprints 2020, 2020120671 (doi: 10.20944/preprints202012.0671.v1).

Abstract

The oncogenic potential of high-risk HPVs is focused on producing the E6 and E7 oncoproteins responsible for disrupting the control of the cell cycle. Epidemiological studies propose the presence of the N29S and H51N variants of the HPV16 E7 protein as a significant association 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 unknown. 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.

Subject Areas

HPV; E7; variants; molecular dynamics simulation

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