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Full-Text Articles in Life Sciences
(1)H, (15)N And (13)C Backbone Resonance Assignments Of The Tpr1 And Tpr2a Domains Of Mouse Sti1., Andrzej Maciejewski, Marco A Prado, Wing-Yiu Choy
(1)H, (15)N And (13)C Backbone Resonance Assignments Of The Tpr1 And Tpr2a Domains Of Mouse Sti1., Andrzej Maciejewski, Marco A Prado, Wing-Yiu Choy
Biochemistry Publications
Hop/STI1 (Hsp-organizing protein/stress-induced-phosphoprotein 1) is a molecular co-chaperone, which coordinates Hsp70 and Hsp90 activity during client protein folding through interactions with its TPR1 and TPR2A domains. Hsp90 substrates include a diverse set of proteins, many of which have been implicated in tumorigenesis. Over-expression of Hsp90 in cancer cells stabilizes mutant oncoproteins promoting cancer cell survival. Disruption of Hsp90 and its co-chaperone machinery has become a promising strategy for the treatment of cancer. STI1 has also been described as a neurotrophic signaling molecule through its interactions with the prion protein (PrP(C)). Here, we report the (1)H, (13)C and (15)N backbone assignments …
Characterization Of The Interaction Between The Parkin Ubiquitin-Like Domain And Ataxin-3 Ubiquitin Interacting Domains, Jane J. Bai
Electronic Thesis and Dissertation Repository
The ubiquitin signaling pathway (USP) consists of hundreds of enzymes which are tightly regulated for proper maintenance of intracellular protein level homeostasis. The main goals of this thesis were to characterize the interaction of two proteins involved in the USP, the E3 ubiquitin ligase called parkin, and the Deubiquitinating (DUB) enzyme, ataxin-3. The effect of disease-state substitutions in the parkin ubiquitin-like domain (UbLD) on the interaction with ataxin-3 was investigated through NMR 1H-15N HSQC titration experiments and affinity binding assays. The three UIM regions in ataxin-3bind the hydrophobic patch of parkin UbLD (KD = 680 μM) …
(1)H, (15)N And (13)C Backbone Resonance Assignments Of The Kelch Domain Of Mouse Keap1., Elio Cino, Jingsong Fan, Daiwen Yang, Wing-Yiu Choy
(1)H, (15)N And (13)C Backbone Resonance Assignments Of The Kelch Domain Of Mouse Keap1., Elio Cino, Jingsong Fan, Daiwen Yang, Wing-Yiu Choy
Biochemistry Publications
Kelch-like ECH-associated Protein 1 (Keap1) is a multi-domain protein that functions as an inhibitor of the transcription factor nuclear factor E2-related factor 2 (Nrf2) in the cellular response to oxidative stress. Under normal conditions, Keap1 binds to Nrf2 via its C-terminal Kelch domain and the interaction ultimately leads to the ubiquitin-dependent degradation of Nrf2. It has been proposed that designing molecules to selectively disrupt the Keap1-Nrf2 interaction can be a potential therapeutic approach for enhancing the expression of cytoprotective genes. Here, we reported the (1)H, (13)C, and (15)N backbone chemical shift assignments of the Kelch domain of mouse Keap1. Further, …