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http://purl.uniprot.org/citations/35115618http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/35115618http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/35115618http://purl.org/dc/terms/identifier"doi:10.1038/s41598-022-05995-1"xsd:string
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/author"Leyva-Vazquez M.A."xsd:string
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/author"Illades-Aguiar B."xsd:string
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/author"Montano S."xsd:string
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/author"Garibay-Cerdenares O.L."xsd:string
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/author"Araujo-Arcos L.E."xsd:string
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/author"Bello-Rios C."xsd:string
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/date"2022"xsd:gYear
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/name"Sci Rep"xsd:string
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/pages"1898"xsd:string
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/title"Molecular insights into the interaction of HPV-16 E6 variants against MAGI-1 PDZ1 domain."xsd:string
http://purl.uniprot.org/citations/35115618http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/35115618http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/35115618
http://purl.uniprot.org/citations/35115618http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/35115618
http://purl.uniprot.org/uniprot/#_A0A455I2N7-mappedCitation-35115618http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35115618
http://purl.uniprot.org/uniprot/#_Q96QZ7-mappedCitation-35115618http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35115618
http://purl.uniprot.org/uniprot/#_V9P4H4-mappedCitation-35115618http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/35115618
http://purl.uniprot.org/uniprot/Q96QZ7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/35115618
http://purl.uniprot.org/uniprot/A0A455I2N7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/35115618
http://purl.uniprot.org/uniprot/V9P4H4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/35115618