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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...
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| Publicado no: | Acta Crystallogr D Biol Crystallogr |
|---|---|
| Main Authors: | , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
International Union of Crystallography
2015
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| Assuntos: | |
| Acesso em linha: | 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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