4I6P

Crystal structure of Par3-NTD domain

4I6P の概要

• エントリーDOI: 10.2210/pdb4i6p/pdb
• 関連するPDBエントリー: 3ZEE
• 分子名称: Partitioning defective 3 homolog (2 entities in total)
• 機能のキーワード: pb1 like motif, duf3534, cell polarity protein, signaling protein
• 由来する生物種: Rattus norvegicus (brown rat,rat,rats)
• 細胞内の位置: Cytoplasm : Q9Z340
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19758.42

構造登録者

Wang, W.,Gao, F.,Gong, W.,Sun, F.,Feng, W. (登録日: 2012-11-29, 公開日: 2013-07-17, 最終更新日: 2023-09-20)

主引用文献

Zhang, Y.,Wang, W.,Chen, J.,Zhang, K.,Gao, F.,Gao, B.,Zhang, S.,Dong, M.,Besenbacher, F.,Gong, W.,Zhang, M.,Sun, F.,Feng, W.
Structural insights into the intrinsic self-assembly of par-3 N-terminal domain.
Structure, 21:997-1006, 2013

PubMed Abstract: 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.

PubMed: 23643951
DOI: 10.1016/j.str.2013.04.004

実験手法

X-RAY DIFFRACTION (2.9 Å)