细胞蛋白质折叠中的分子伴侣
Molecular chaperones in cellular protein folding.
作者信息
Hartl F U, Martin J
机构信息
Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
出版信息
Curr Opin Struct Biol. 1995 Feb;5(1):92-102. doi: 10.1016/0959-440x(95)80014-r.
PMID:7773752
Abstract
Protein folding in the cell requires molecular chaperones. The chaperone proteins of the hsp70 and hsp60 (chaperonin) classes stabilize unfolded or partially folded polypeptides, thereby preventing aggregation, and mediate folding to the native state in ATP-dependent reactions. Recent advances include a more detailed understanding of the mechanistic principles of hsp70 and hsp60 action, the solution of the crystal structure of the chaperonin GroEL, and the definition of pathways of chaperone-mediated protein folding.
摘要
细胞中的蛋白质折叠需要分子伴侣。热休克蛋白70（hsp70）和热休克蛋白60（伴侣蛋白）家族的伴侣蛋白可稳定未折叠或部分折叠的多肽，从而防止聚集，并在ATP依赖的反应中介导其折叠成天然状态。最近的进展包括对hsp70和hsp60作用机制原理的更详细了解、伴侣蛋白GroEL晶体结构的解析以及伴侣蛋白介导的蛋白质折叠途径的确定。
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