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Structure of the E6/E6AP/p53 Complex in Human Papillomavirus
Author(s) -
Fassler Amy,
Bhat Tara,
Rens Davis,
Chojnacki Kennan,
Neil Uma
Publication year - 2020
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.2020.34.s1.03364
Subject(s) - ubiquitin ligase , suppressor , docking (animal) , ubiquitin , microbiology and biotechnology , function (biology) , chemistry , p53 protein , cancer research , biology , apoptosis , computational biology , cancer , biochemistry , medicine , genetics , gene , nursing
Human Papillomavirus (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. The E6 oncoprotein directly inhibits p53s function by attaching itself to a ubiquitin ligase, E6AP, which in turn forms a complex with p53. E6 and E6AP form a heterodimer by binding at a leucine‐rich docking site, known as the LxxLL motif. The heterodimer then forms a binding pocket with p53, which is the cause of the inactivation of p53 function. Researchers are attempting to identify potential binding pocket function in the complex in order to form a protein inhibition mechanism that can block further proliferation of cervical cancer. Understanding the interactions of the E6/E6AP/p53 complex is leading to the development of unique antiviral and chemotherapeutic agents for cervical cancer. The Marshfield High School MSOE Center for BioMolecular Modellng for SMART Team used 3D modelling and printing technology to examine the structure‐function relationships of the E6/E6AP/p53 complex. Support or Funding Information Marshfield Clinic LaboratoriesMSOE Center for BioMolecular ModelingMarshfield Area Community Foundation