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A novel conformation of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90
Hsp90, an essential eukaryotic chaperone, depends upon its intrinsic ATPase activity for function. Crystal structures of the bacterial Hsp90 homolog, HtpG, and the yeast Hsp90 reveal large domain rearrangements between the nucleotide-free and the nucleotide-bound forms. Using small-angle x-ray scatt...
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| Hauptverfasser: | , , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
2008
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2600884/ https://ncbi.nlm.nih.gov/pubmed/18462680 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2008.01.021 |
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