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N-terminal domain of αB-crystallin provides a conformational switch for multimerization and structural heterogeneity
The small heat shock protein (sHSP) αB-crystallin (αB) plays a key role in the cellular protection system against stress. For decades, high-resolution structural studies on heterogeneous sHSPs have been confounded by the polydisperse nature of αB oligomers. We present an atomic-level model of full-l...
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| Päätekijät: | , , , , , , , |
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| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
National Academy of Sciences
2011
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3081008/ https://ncbi.nlm.nih.gov/pubmed/21464278 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1014656108 |
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