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Human Papilloma Virus E6Protein Binding to P53
Author(s) -
Fassler Amy,
Bhat Tara,
Chojnacki Kennan,
Rens Davis,
Shah Ruhi
Publication year - 2021
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2021.35.s1.02730
Subject(s) - suppressor , capsid , telomerase , cancer research , cervical cancer , hela , p53 protein , cancer , apoptosis , biology , virus , virology , cell , genetics , gene
Human Papilloma Virus (HPV) is the most common sexually transmitted pathogen in humans and the primary cause of cervical cancer. The tumor suppressor p53, in its normal state, regulates cell growth and survival through mechanisms including DNA repair and apoptosis. When p53 binds to the HPV E6 oncoprotein, a binding pocket is formed, causing partial inactivation of the tumor suppressor. E6 is found in the L1 capsid protein of HPV, and directly causes the degradation of p53, as well as the activation of telomerase[, a ribonucleic enzyme that prevents the decline in chromosome function, and therefore allows HPV infected cells proliferate leading to the development of cancer. Researchers are attempting to identify potential binding pockets in E6 in hopes of forming a protein inhibition mechanism that can block further proliferation of cervical cancer. Understanding the regulation of E6 in human papillomavirus will allow the formation of vaccinations of higher specificity as well as treatments for cervical cancer. The Marshfield High School MSOE Center for BioMolecular Modelling for SMART Team used 3D Modelling and printing technology to examine structure‐ function relationships of the E6 oncoprotein and p53 tumor suppressor.