3lra
From Proteopedia
Structural Basis for Assembling a Human Tripartite Complex Dlg1-MPP7-Mals3
Structural highlights
Function[DLG1_HUMAN] Essential multidomain scaffolding protein required for normal development (By similarity). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells. May play a role in adherens junction assembly, signal transduction, cell proliferation, synaptogenesis and lymphocyte activation. Regulates the excitability of cardiac myocytes by modulating the functional expression of Kv4 channels. Functional regulator of Kv1.5 channel.[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedThe 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 alphaA-alphaB and helix alphaB 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.-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. Structural basis for tandem L27 domain-mediated polymerization.,Yang X, Xie X, Chen L, Zhou H, Wang Z, Zhao W, Tian R, Zhang R, Tian C, Long J, Shen Y FASEB J. 2010 Aug 11. PMID:20702775[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Human | Long, J | Shen, Y | Xie, X | Yang, X | Cell junction | Cell membrane | Endoplasmic reticulum | Exocytosis | Host-virus interaction | L27 tetramer | Membrane protein | Postsynaptic cell membrane | Protein transport | Sh3 domain | Synapse | Synaptosome | Tight junction | Transport | Tripartite complex
