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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Detalles Bibliográficos
Autores principales: Morgan, Rhodri M. L., Pal, Mohinder, Roe, S. Mark, Pearl, Laurence H., Prodromou, Chrisostomos
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2015
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4427203/
https://www.ncbi.nlm.nih.gov/pubmed/25945584
http://dx.doi.org/10.1107/S1399004715004551

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4427203/
https://www.ncbi.nlm.nih.gov/pubmed/25945584
http://dx.doi.org/10.1107/S1399004715004551

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