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Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles
The Hsp70 chaperone system is integrated into a myriad of biochemical processes that are critical for cellular proteostasis. Although detailed pictures of Hsp70 bound with peptides have emerged, correspondingly detailed structural information on complexes with folding-competent substrates remains la...
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| Publicado en: | eLife |
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| Autores principales: | , , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
eLife Sciences Publications, Ltd
2017
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5511010/ https://ncbi.nlm.nih.gov/pubmed/28708484 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.7554/eLife.28030 |
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