Mogk Axel, Bukau Bernd
1ZMBH, Universität Heidelberg, Im Neuenheimer Feld 282, D-69120, Heidelberg, Germany.
Curr Biol. 2004 Jan 20;14(2):R78-80. doi: 10.1016/j.cub.2003.12.051.
The ring-forming molecular chaperone Hsp104/ClpB is a member of the AAA+ protein family which rescues proteins from aggregated states. The newly determined crystal structure of ClpB provides new insights into the mechanism of protein disaggregation, suggesting a crowbar activity mediated by a unique coiled-coil domain.
形成环状的分子伴侣Hsp104/ClpB是AAA+蛋白家族的成员，可将蛋白质从聚集状态中解救出来。新测定的ClpB晶体结构为蛋白质解聚机制提供了新见解，表明一种由独特的卷曲螺旋结构域介导的撬棍活性。
