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3UIT

Overall structure of Patj/Pals1/Mals complex

Summary for 3UIT
Entry DOI10.2210/pdb3uit/pdb
DescriptorInaD-like protein, MAGUK p55 subfamily member 5, Protein lin-7 homolog B, ACETATE ION (3 entities in total)
Functional Keywordsl27 domain, cell polarization, cell adhesion
Biological sourceMus musculus (mouse, human, rat)
More
Cellular locationCell membrane ; Peripheral membrane protein : Q9Z252
Total number of polymer chains4
Total formula weight120605.72
Authors
Zhang, J.,Yang, X.,Long, J.,Shen, Y. (deposition date: 2011-11-06, release date: 2012-02-22, Last modification date: 2024-03-20)
Primary citationZhang, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.05 Å)
Structure validation

243531

数据于2025-10-22公开中

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