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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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| Publicado no: | Cell Rep |
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| Main Authors: | , , , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2020
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| Assuntos: | |
| Acesso em linha: | 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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