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Chaperone-client interactions: Non-specificity engenders multifunctionality
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DOI：10.1074/jbc.R117.796862.png)
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摘要
En 中文
Here, we provide an overview of the different mechanisms whereby three different chaperones, Spy, Hsp70, and Hsp60, interact with folding proteins, and we discuss how these chaperones may guide the folding process. Available evidence suggests that even a single chaperone can use many mechanisms to aid in protein folding, most likely due to the need for most chaperones to bind clients promiscuously. Chaperone mechanism may be better understood by always considering it in the context of the client's folding pathway and biological function.
Keyword:
FUSION ONCOPROTEIN AML1-ETO
ESCHERICHIA-COLI
MOLECULAR CHAPERONE
SUBSTRATE RECOGNITION
HSP70 CHAPERONES
ATP HYDROLYSIS
GROEL-GROES
PROTEIN
BINDING
TRIC/CCT
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期刊
IF:
3.9
论文数:
11.2W
被引数:
28.3W
机构
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