例如:"lncRNA", "apoptosis", "WRKY"

Structural insights into the intrinsic self-assembly of Par-3 N-terminal domain.

Structure. 2013 Jun 4;21(6):997-1006. Epub 2013 May 02
Yan Zhang 1 , Wenjuan Wang , Jia Chen , Kai Zhang , Feng Gao , Bingquan Gao , Shuai Zhang , Mingdong Dong , Flemming Besenbacher , Weimin Gong , Mingjie Zhang , Fei Sun , Wei Feng
Yan Zhang 1 , Wenjuan Wang , Jia Chen , Kai Zhang , Feng Gao , Bingquan Gao , Shuai Zhang , Mingdong Dong , Flemming Besenbacher , Weimin Gong , Mingjie Zhang , Fei Sun , Wei Feng
+ et al

[No authors listed]

Author information
  • 1 National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing 100101, China.

摘要


Par-3, the central organizer of the Par-3/Par-6/atypical protein kinase C complex, is a multimodular scaffold protein that is essential for cell polarity establishment and maintenance. The N-terminal domain (NTD) of Par-3 is capable of self-association to form filament-like structures, although the underlying mechanism is poorly understood. Here, we determined the crystal structure of Par-3 NTD and solved the filament structure by cryoelectron microscopy. We found that an intrinsic "front-to-back" interaction mode is important for Par-3 NTD self-association and that both the lateral and longitudinal packing within the filament are mediated by electrostatic interactions. Disruptions of the lateral or longitudinal packing significantly impaired Par-3 NTD self-association and thereby impacted the Par-3-mediated epithelial polarization. We finally demonstrated that a Par-3 NTD-like domain from histidine ammonia-lyase also harbors a similar self-association capacity. This work unequivocally provides the structural basis for Par-3 NTD self-association and characterizes one type of protein domain that can self-assemble via electrostatic interactions.