Conformational dynamics of the Rpt6 ATPase in proteasome assembly and Rpn14 binding

Juxtaposed to either or both ends of the proteasome core particle (CP) can exist a 19S regulatory particle (RP) that recognizes and prepares ubiquitinated proteins for proteolysis. RP triphosphatase proteins (Rpt1-Rpt6), which are critical for substrate translocation into the CP, bind chaperone-like...

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Hlavní autoři: Ehlinger, Aaron, Park, Soyeon, Fahmy, Amr, Lary, Jeffrey W., Cole, James L., Finley, Daniel, Walters, Kylie J.
Médium: Artigo
Jazyk:Inglês
Vydáno: 2013
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Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3670613/
https://ncbi.nlm.nih.gov/pubmed/23562395
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2013.02.021
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