Version 1
: Received: 3 September 2021 / Approved: 6 September 2021 / Online: 6 September 2021 (13:51:17 CEST)
How to cite:
Araujo- Arcos, L.E.; Bello-Rios, C.; Garibay- Cerdenares, O.L.; Leyva-Vázquez, M.A.; Montaño, S.; Illades-Aguiar, B. Insights in the Interaction of HPV-16 E6 and Its Variants (E-G350, E-A176/G350, E-C188/G350, AAa and AAc) with MAGI-1. Preprints2021, 2021090101. https://doi.org/10.20944/preprints202109.0101.v1
Araujo- Arcos, L.E.; Bello-Rios, C.; Garibay- Cerdenares, O.L.; Leyva-Vázquez, M.A.; Montaño, S.; Illades-Aguiar, B. Insights in the Interaction of HPV-16 E6 and Its Variants (E-G350, E-A176/G350, E-C188/G350, AAa and AAc) with MAGI-1. Preprints 2021, 2021090101. https://doi.org/10.20944/preprints202109.0101.v1
Araujo- Arcos, L.E.; Bello-Rios, C.; Garibay- Cerdenares, O.L.; Leyva-Vázquez, M.A.; Montaño, S.; Illades-Aguiar, B. Insights in the Interaction of HPV-16 E6 and Its Variants (E-G350, E-A176/G350, E-C188/G350, AAa and AAc) with MAGI-1. Preprints2021, 2021090101. https://doi.org/10.20944/preprints202109.0101.v1
APA Style
Araujo- Arcos, L.E., Bello-Rios, C., Garibay- Cerdenares, O.L., Leyva-Vázquez, M.A., Montaño, S., & Illades-Aguiar, B. (2021). Insights in the Interaction of HPV-16 E6 and Its Variants (E-G350, E-A176/G350, E-C188/G350, AAa and AAc) with MAGI-1. Preprints. https://doi.org/10.20944/preprints202109.0101.v1
Chicago/Turabian Style
Araujo- Arcos, L.E., Sarita Montaño and Berenice Illades-Aguiar. 2021 "Insights in the Interaction of HPV-16 E6 and Its Variants (E-G350, E-A176/G350, E-C188/G350, AAa and AAc) with MAGI-1" Preprints. https://doi.org/10.20944/preprints202109.0101.v1
Abstract
Oncogenic protein E6 from Human Papilloma Virus 16 (HPV-16) mediates the degradation of Membrane-associated guanylate kinase with inverted domain structure-1 (MAGI-1), throughout the interaction of its protein binding motif (PBM) with the Discs-large homologous regions 1 (PDZ1) domain of MAG1-1. Generic variation in the E6 gene that translates to changes in the protein’s amino acidic sequence modifies the interaction of E6 with the cellular protein MAGI-1. MAGI-1 is a scaffolding protein found at tight junctions of epithelial cells, where it interacts with a variety of proteins regulating signaling pathways. MAGI-1 is a multidomain protein containing two WW (rsp-domain-9), one guanylate kinase-like, and six PDZ domains. PDZ domains played an important role in the function of MAGI-1 and served as targets for several viral proteins including the HPV-16 E6. The aim of this work was to evaluate, with an in silico approach, employing molecular dynamics simulation and protein-protein docking, the interaction of the intragenic variants E-G350 (L83V), E-C188/G350 (E29Q/L83V), E-A176/G350 (D25N/L83V), E6-AAa (Q14H/H78Y/83V) y E6-AAc (Q14H/I27RH78Y/L83V) and E6-reference of HPV-16 with MAGI-1. We found that variants E-G350, E-C188/G350, E-A176/G350, AAa and AAc increase their affinity to our two models of MAGI-1 compared to E6-reference.
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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