3LRA

Structural Basis for Assembling a Human Tripartite Complex Dlg1-MPP7-Mals3

Summary for 3LRA

• Entry DOI: 10.2210/pdb3lra/pdb
• Descriptor: Disks large homolog 1, MAGUK p55 subfamily member 7, Protein lin-7 homolog C (2 entities in total)
• Functional Keywords: tripartite complex, l27 tetramer, cell junction, cell membrane, endoplasmic reticulum, host-virus interaction, postsynaptic cell membrane, sh3 domain, synapse, tight junction, exocytosis, protein transport, synaptosome, transport, membrane protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane ; Peripheral membrane protein : Q9NUP9
• Total number of polymer chains: 1
• Total formula weight: 29164.17

Authors

Yang, X.,Xie, X.,Shen, Y.,Long, J. (deposition date: 2010-02-10, release date: 2010-11-17, Last modification date: 2024-03-20)

Primary citation

Yang, X.,Xie, X.,Chen, L.,Zhou, H.,Wang, Z.,Zhao, W.,Tian, R.,Zhang, R.,Tian, C.,Long, J.,Shen, Y.
Structural basis for tandem L27 domain-mediated polymerization
Faseb J., 24:4806-4815, 2010

PubMed Abstract: The establishment of epithelial cell polarity requires the assembly of multiprotein complexes and is crucial during epithelial morphogenesis. Three scaffolding proteins, Dlg1, MPP7, and Mals3, can be assembled to form a complex that functions in the establishment and maintenance of apicobasal polarity in epithelial tissues through their L27 domains. Here we report the crystal structure of a 4-L27-domain complex derived from the human tripartite complex Dlg1-MPP7-Mals3 in combination with paramagnetic relaxation enhancement measurements. The heterotrimer consists of 2 pairs of heterodimeric L27 domains. These 2 dimers are asymmetric due to the large difference between the N- and C-terminal tandem L27 domain of MPP7. Structural analysis combined with biochemical experiments further reveals that the loop αA-αB and helix αB of the C-terminal L27 domain of MPP7 play a critical role in assembling the entire tripartite complex, suggesting a synergistic tandem L27-mediated assembling event.

PubMed: 20702775
DOI: 10.1096/fj.10-163857

Experimental method

X-RAY DIFFRACTION (2.95 Å)