3UIT

Overall structure of Patj/Pals1/Mals complex

3UIT の概要

• エントリーDOI: 10.2210/pdb3uit/pdb
• 分子名称: InaD-like protein, MAGUK p55 subfamily member 5, Protein lin-7 homolog B, ACETATE ION (3 entities in total)
• 機能のキーワード: l27 domain, cell polarization, cell adhesion
• 由来する生物種: Mus musculus (mouse, human, rat); 詳細
• 細胞内の位置: Cell membrane ; Peripheral membrane protein : Q9Z252
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 120605.72

構造登録者

Zhang, J.,Yang, X.,Long, J.,Shen, Y. (登録日: 2011-11-06, 公開日: 2012-02-22, 最終更新日: 2024-03-20)

主引用文献

Zhang, J.,Yang, X.,Wang, Z.,Zhou, H.,Xie, X.,Shen, Y.,Long, J.
Structure of an L27 domain heterotrimer from cell polarity complex Patj/Pals1/Mals2 reveals mutually independent L27 domain assembly mode
J.Biol.Chem., 287:11132-11140, 2012

PubMed Abstract: The assembly of supramolecular complexes in multidomain scaffold proteins is crucial for the control of cell polarity. The scaffold protein of protein associated with Lin-7 1 (Pals1) forms a complex with two other scaffold proteins, Pals-associated tight junction protein (Patj) and mammalian homolog-2 of Lin-7 (Mals2), through its tandem Lin-2 and Lin-7 (L27) domains to regulate apical-basal polarity. Here, we report the crystal structure of a 4-L27 domain-containing heterotrimer derived from the tripartite complex Patj/Pals1/Mals2. The heterotrimer consists of two cognate pairs of heterodimeric L27 domains with similar conformations. Structural analysis and biochemical data further show that the dimers assemble mutually independently. Additionally, such mutually independent assembly of the two heterodimers can be observed in another tripartite complex, Disks large homolog 1 (DLG1)/calcium-calmodulin-dependent serine protein kinase (CASK)/Mals2. Our results reveal a novel mechanism for tandem L27 domain-mediated, supramolecular complex assembly with a mutually independent mode.

PubMed: 22337881
DOI: 10.1074/jbc.M111.321216

実験手法

X-RAY DIFFRACTION (2.05 Å)