The Charged Linker Modulates the Conformations and Molecular Interactions of Hsp90

The molecular chaperone Hsp90 supports the functional activity of specific substrate proteins (clients). For client processing, the Hsp90 dimer undergoes a series of ATP‐driven conformational rearrangements. Flexible linkers connecting the three domains of Hsp90 are crucial to enable dynamic arrange...

Descripción completa

Detalles Bibliográficos
Autores principales: López, Abraham, Elimelech, Annika R., Klimm, Karolin, Sattler, Michael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
Materias:
Full Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8048802/
https://www.ncbi.nlm.nih.gov/pubmed/33147371
http://dx.doi.org/10.1002/cbic.202000699

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8048802/
https://www.ncbi.nlm.nih.gov/pubmed/33147371
http://dx.doi.org/10.1002/cbic.202000699

Ejemplares similares