Literature summary for 3.6.4.10 extracted from

Colombo, G.; Morra, G.; Meli, M.; Verkhivker, G.
Understanding ligand-based modulation of the Hsp90 molecular chaperone dynamics at atomic resolution (2008), Proc. Natl. Acad. Sci. USA, 105, 7976-7981.

Crystallization (Commentary)

Crystallization (Comment)	Organism
atomic resolution analysis of the Hsp90 N-terminal domain binding energy landscape by simulating protein dynamics with binding partners such as ATP, ADP, shepherdin. The activity of the molecular chaperone may be linked to local folding-unfolding transitions and conformational switching of the active site lid upon binding and differences in the underlying protein dynamics as a function of the binding partner	Homo sapiens

Crystallization (Comment)

Organism

atomic resolution analysis of the Hsp90 N-terminal domain binding energy landscape by simulating protein dynamics with binding partners such as ATP, ADP, shepherdin. The activity of the molecular chaperone may be linked to local folding-unfolding transitions and conformational switching of the active site lid upon binding and differences in the underlying protein dynamics as a function of the binding partner

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	isoform Hsp90	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)