Structures of Gα Proteins in Complex with Their Chaperone Reveal Quality Control Mechanisms

Many chaperones promote nascent polypeptide folding followed by substrate release through ATP-dependent conformational changes. Here we show cryoEM structures of Gα subunit folding intermediates in complex with full-length Ric-8A, a unique chaperone-client system in which substrate release is facili...

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Dettagli Bibliografici
Pubblicato in:Cell Rep
Autori principali: Seven, Alpay Burak, Hilger, Daniel, Papasergi-Scott, Makaía M., Zhang, Li, Qu, Qianhui, Kobilka, Brian K., Tall, Gregory G., Skiniotis, Georgios
Natura: Artigo
Lingua:Inglês
Pubblicazione: 2020
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Article
Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC7192526/
https://ncbi.nlm.nih.gov/pubmed/32126208
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.celrep.2020.02.086
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