ArticleScientific reports2022
Molecular insights into the interaction of HPV-16 E6 variants against MAGI-1 PDZ1 domain.
Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Molecular Insights from Differential Proteomic Profiling of Premalignant Cervical Lesions and Cervical Cancer.Pathogens (Basel, Switzerland) · 2026Article
- Article
- Molecular Dynamics and Docking Reveal Enhanced Binding of HPV16 E6 Asian American Variants To non-phosphorylated DLG1.Cell biochemistry and biophysics · 2026Article
- Targeted degradation of the HPV oncoprotein E6 reduces tumor burden in cervical cancer.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Article
- Identification of novel therapeutic inhibitors against E6 and E7 oncogenes of HPV-16 associated with cervical cancer.PloS one · 2025Article
- The role of HR-HPV integration in the progression of premalignant lesions into different cancer types.Heliyon · 2024Review
- Article
- SRC inhibition enables formation of a growth suppressive MAGI1-PP2A complex in isocitrate dehydrogenase-mutant cholangiocarcinoma.Science translational medicine · 2024Article
- Prediction of motif-mediated viral mimicry through the integration of host-pathogen interactions.Archives of microbiology · 2024Article
- Discovery of reactive peptide inhibitors of human papillomavirus oncoprotein E6.Chemical science · 2023Article
- The T350G Variation of Human Papillomavirus 16Viruses · 2022Article
- Epidemiology and Molecular Biology of HPV Variants in Cervical Cancer: The State of the Art in Mexico.International journal of molecular sciences · 2022Review
- Molecular Mechanisms of HIV Protease Inhibitors Against HPV-Associated Cervical Cancer: Restoration ofFrontiers in molecular biosciences · 2022Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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