笼状结构：GroEL-GroES-(ADP)7晶体结构中的不对称性
La cage aux fold: asymmetry in the crystal structure of GroEL-GroES-(ADP)7.
作者信息
Harrison C J
机构信息
Laboratories of Molecular Biophysics, Howard Hughes Medical Institute, Rockefeller University, NY 10021, USA.
出版信息
Structure. 1997 Oct 15;5(10):1261-4. doi: 10.1016/s0969-2126(97)00277-3.
PMID:9351802
Abstract
The structure of the molecular chaperone GroEL from Escherichia coli in complex with GroES and seven ADP molecules has recently been reported to 3 A resolution. The structure illustrates how the cavity of GroEL is converted from a hydrophobic environment, suitable for binding unfolded polypeptides, to a much larger hydrophilic environment suitable for refolding proteins.
摘要
最近有报道称，来自大肠杆菌的分子伴侣GroEL与GroES及七个ADP分子形成复合物的结构已解析到3埃的分辨率。该结构展示了GroEL的腔是如何从适合结合未折叠多肽的疏水环境转变为适合蛋白质重折叠的更大的亲水环境的。
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