Cyr Douglas M
Department of Cell and Developmental Biology, School of Medicine, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Cell. 2008 Jun 13;133(6):945-7. doi: 10.1016/j.cell.2008.05.036.
Molecular chaperones such as heat shock protein 70 (Hsp70) are crucial for protein folding. Crystal structures of Hsp70 in a complex with the nucleotide exchange factor (NEF) Hsp110 reported in this issue of Cell (Polier et al., 2008) and in Molecular Cell (Schuermann et al., 2008) provide new insights into how NEF action specifies Hsp70 cellular function.
诸如热休克蛋白70(Hsp70)之类的分子伴侣对蛋白质折叠至关重要。本期《细胞》(Polier等人,2008年)和《分子细胞》(Schuermann等人,2008年)报道的与核苷酸交换因子(NEF)Hsp110形成复合物的Hsp70晶体结构,为NEF作用如何决定Hsp70的细胞功能提供了新的见解。