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-Structure paper
タイトル | Structural insights into the intrinsic self-assembly of Par-3 N-terminal domain. |
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ジャーナル・号・ページ | Structure, Vol. 21, Issue 6, Page 997-991006, Year 2013 |
掲載日 | 2013年6月4日 |
![]() | Yan Zhang / Wenjuan Wang / Jia Chen / Kai Zhang / Feng Gao / Bingquan Gao / Shuai Zhang / Mingdong Dong / Flemming Besenbacher / Weimin Gong / Mingjie Zhang / Fei Sun / Wei Feng / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (らせん対称) / X線回折 |
解像度 | 2.9 - 6.1 Å |
構造データ | EMDB-2237: Electron cyro-microscopy helical reconstruction of Par-3 N-terminal domain ![]() PDB-4i6p: |
化合物 | ![]() ChemComp-HOH: |
由来 |
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![]() | CELL CYCLE / SIGNALING PROTEIN / PB1 like motif / DUF3534 / Cell polarity protein |