3RO3

crystal structure of LGN/mInscuteable complex

3RO3 の概要

• エントリーDOI: 10.2210/pdb3ro3/pdb
• 関連するPDBエントリー: 3RO2
• 分子名称: G-protein-signaling modulator 2, peptide of Protein inscuteable homolog, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: asymmetric cell division, protein binding
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Cytoplasm (By similarity): Q8VDU0; Cytoplasm: Q3HNM7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21478.27

構造登録者

Zhu, J.,Wen, W.,Shang, Y.,Wei, Z.,Pan, Z.,Wang, W.,Zhang, M. (登録日: 2011-04-25, 公開日: 2012-03-07, 最終更新日: 2024-03-20)

主引用文献

Zhu, J.,Wen, W.,Zheng, Z.,Shang, Y.,Wei, Z.,Xiao, Z.,Pan, Z.,Du, Q.,Wang, W.,Zhang, M.
LGN/mInsc and LGN/NuMA complex structures suggest distinct functions in asymmetric cell division for the Par3/mInsc/LGN and G[alpha]i/LGN/NuMA pathways
Mol.Cell, 43:418-431, 2011

PubMed Abstract: Asymmetric cell division requires the establishment of cortical cell polarity and the orientation of the mitotic spindle along the axis of cell polarity. Evidence from invertebrates demonstrates that the Par3/Par6/aPKC and NuMA/LGN/Gαi complexes, which are thought to be physically linked by the adaptor protein mInscuteable (mInsc), play indispensable roles in this process. However, the molecular basis for the binding of LGN to NuMA and mInsc is poorly understood. The high-resolution structures of the LGN/NuMA and LGN/mInsc complexes presented here provide mechanistic insights into the distinct and highly specific interactions of the LGN TPRs with mInsc and NuMA. Structural comparisons, together with biochemical and cell biology studies, demonstrate that the interactions of NuMA and mInsc with LGN are mutually exclusive, with mInsc binding preferentially. Our results suggest that the Par3/mInsc/LGN and NuMA/LGN/Gαi complexes play sequential and partially overlapping roles in asymmetric cell division.

PubMed: 21816348
DOI: 10.1016/j.molcel.2011.07.011

実験手法

X-RAY DIFFRACTION (1.1 Å)