STRUCTURAL AND FUNCTIONAL STUDIES OF CYCLIC K48-LINKED DIUBIQUITIN

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dc.contributor.advisorFushman, Daviden_US
dc.contributor.authorSundar, Adithyaen_US
dc.contributor.departmentBiochemistryen_US
dc.contributor.publisherDigital Repository at the University of Marylanden_US
dc.contributor.publisherUniversity of Maryland (College Park, Md.)en_US
dc.date.accessioned2016-09-08T05:42:22Z
dc.date.available2016-09-08T05:42:22Z
dc.date.issued2016en_US
dc.description.abstractK48-linked di-ubiquitin exists in a dynamic equilibrium between open and closed states. The structure of K48-Ub2 in the closed conformation features a hydrophobic interface formed between the two Ub domains. The same hydrophobic residues at the interface are involved in binding to ubiquitin-associated (UBA) domains. Cyclization of K48-Ub2 should limit the range of conformations available for such interactions. Interestingly, cyclic K48-linked Ub2 (cycUb2) has been found in vivo and can be isolated in vitro to study its structure and dynamics. In this study, a crystal structure of cycUb2 was obtained, and the dynamics of cycUb2 were characterized by solution NMR. The crystal structure of cycUb2, which is in agreement with solution NMR data, is closed with the hydrophobic patches of each Ub domain buried at the interface. Despite its structural constraints, cycUb2 was still able to interact with UBA domains, albeit with lower affinity.en_US
dc.identifierhttps://doi.org/10.13016/M2XN6V
dc.identifier.urihttp://hdl.handle.net/1903/18782
dc.language.isoenen_US
dc.subject.pqcontrolledBiochemistryen_US
dc.subject.pquncontrolledcyclic K48-linked di-ubiquitinen_US
dc.subject.pquncontrolleddynamicsen_US
dc.subject.pquncontrolledprotein NMRen_US
dc.subject.pquncontrolledstructureen_US
dc.subject.pquncontrolledubiquitinen_US
dc.titleSTRUCTURAL AND FUNCTIONAL STUDIES OF CYCLIC K48-LINKED DIUBIQUITINen_US
dc.typeThesisen_US

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