Kelley W L
Département de Biochimie Médicale, CMU-Université de Genève, 1 rue Michel-Servet, 1211 Genève 4, Switzerland.
Curr Biol. 1999 Apr 22;9(8):R305-8. doi: 10.1016/s0960-9822(99)80185-7.
Molecular chaperones of the heat shock protein 70 (Hsp70) variety facilitate protein folding and assembly. They are assisted in this role by their Hsp40 partners, and recent studies have shed new light on how the 'J domains' of these 'cochaperones' activate substrate binding by Hsp70 molecules.
热休克蛋白70(Hsp70)家族的分子伴侣促进蛋白质折叠和组装。它们在这一作用中得到其Hsp40伴侣的协助,并且最近的研究为这些“共伴侣”的“J结构域”如何激活Hsp70分子的底物结合提供了新的线索。