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Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexes
Specific co-chaperone adaptors facilitate the recruitment of client proteins to the Hsp90 system. Tah1 binds the C-terminal conserved MEEVD motif of Hsp90, thus linking an eclectic set of client proteins to the R2TP complex for their assembly and regulation by Hsp90. Rather than the normal complemen...
Tallennettuna:
| Julkaisussa: | Acta Crystallogr D Biol Crystallogr |
|---|---|
| Päätekijät: | , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
International Union of Crystallography
2015
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4427203/ https://ncbi.nlm.nih.gov/pubmed/25945584 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1399004715004551 |
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