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Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity
Small heat-shock proteins (sHsps) prevent aggregation of thermosensitive client proteins in a first line of defense against cellular stress. The mechanisms by which they perform this function have been hard to define due to limited structural information; currently, there is only one high-resolution...
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| Publicado en: | J Biol Chem |
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| Autores principales: | , , , , , , , , , , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Biochemistry and Molecular Biology
2017
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5427286/ https://ncbi.nlm.nih.gov/pubmed/28325834 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M116.766816 |
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