热休克蛋白90
伴侣(临床)
蛋白质折叠
热休克蛋白70
折叠(DSP实现)
生物物理学
细胞生物学
共同伴侣
血浆蛋白结合
变构调节
结合位点
ATP酶
蛋白质结构
化学
生物化学
生物
热休克蛋白
受体
酶
工程类
电气工程
病理
基因
医学
作者
G. Elif Karagöz,Stefan Rüdiger
标识
DOI:10.1016/j.tibs.2014.12.002
摘要
The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the stability of select proteins. Emerging data explain how Hsp90 achieves client specificity and its role in the cellular chaperone cascade. Interestingly, Hsp90 has an extended substrate binding interface that crosses domain boundaries, exhibiting specificity for proteins with hydrophobic residues spread over a large area regardless of whether they are disordered, partly folded, or even folded. This specificity principle ensures that clients preferentially bind to Hsp70 early on in the folding path, but downstream folding intermediates bind Hsp90. Discussed here, the emerging model is that the Hsp90 ATPase does not modulate client affinity but instead controls substrate influx from Hsp70.
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