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dc.contributor.advisorKlevit, Rachel E
dc.contributor.authorLoutey, Dana Elizabeth
dc.date.accessioned2019-05-02T23:17:37Z
dc.date.available2019-05-02T23:17:37Z
dc.date.submitted2019
dc.identifier.otherLoutey_washington_0250O_19779.pdf
dc.identifier.urihttp://hdl.handle.net/1773/43641
dc.descriptionThesis (Master's)--University of Washington, 2019
dc.description.abstractThe human proteome contains over forty ubiquitin-conjugating enzymes, each harboring a conserved core domain. Despite their structural similarities, E2s must discriminate between hundreds of E3 ligases to interact specifically with their cognate partners. Structural and functional characterization of E2s in the last few decades has revealed unique mechanistic details for each E2 studied thus far, but no universal rule appears to govern how E2 enzymes specifically recognize their cognate binding partners. Many E2s remain uncharacterized and promise to reveal novel strategies by which these apparently simple enzymes achieve specificity in both E3 binding and Ub transfer. Ube2H is a human E2 enzyme with an uncharacterized C-terminal extension of 32 residues. The extension is phylogenetically conserved, but its function is unknown. In this thesis, I employ biophysical and biochemical techniques to investigate the structural and biochemical function of Ube2H’s C-terminal extension, both alone and in the presence of putative E3 ligases and binding partners.
dc.format.mimetypeapplication/pdf
dc.language.isoen_US
dc.rightsnone
dc.subjectProtein NMR
dc.subjectStructural biology
dc.subjectUbe2H
dc.subjectUbiquitin-conjugating enzyme
dc.subjectUbiquitylation
dc.subjectBiochemistry
dc.subjectBiophysics
dc.subject.otherBiological chemistry
dc.titleStructural and Functional Characterization of Ube2H, a Ubiquitin-Conjugating Enzyme with a C-terminal Extension
dc.typeThesis
dc.embargo.termsOpen Access


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