Intra- and Intermonomer Interactions Are Required to Synergistically Facilitate ATP Hydrolysis in Hsp90

Nucleotide-dependent conformational changes of the constitutively dimeric molecular chaperone Hsp90 are integral to its molecular mechanism. Recent full-length crystal structures (Protein Data Bank codes 2IOQ, 2CG9, AND 2IOP) of Hsp90 homologs reveal large scale quaternary domain rearrangements upon...

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Detalles Bibliográficos
Autores principales: Cunningham, Christian N., Krukenberg, Kristin A., Agard, David A.
Formato: Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2008
Materias:
Protein Structure and Folding
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2475720/
https://www.ncbi.nlm.nih.gov/pubmed/18492664
http://dx.doi.org/10.1074/jbc.M800046200

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2475720/
https://www.ncbi.nlm.nih.gov/pubmed/18492664
http://dx.doi.org/10.1074/jbc.M800046200

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