3w9y
From Proteopedia
Crystal structure of the human DLG1 guanylate kinase domain
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 PubMedDiscs large homolog 1 (DLG1/SAP97) is involved in the development and regulation of neuronal and immunological synapses. DLG1 is a member of the membrane associated guanylate kinase (MAGUK) family of proteins, which function as molecular scaffolds. The C-terminal guanylate kinase (GK) domain of DLG1 binds peptides with a phosphorylated serine residue. In this study, we solved the crystal structure of the GK domain of human DLG1. The C-terminal tail of DLG1 is bound to the peptide-binding site of an adjacent symmetry-related DLG1 GK molecule. The binding direction of the C-terminal tail to the peptide-binding site is opposite to that of the phosphorylated LGN peptide in complex with the rat DLG1 GK domain. The C-terminal tail forms a 310 helix, which is also different from the conformation of the phosphorylated LGN peptide. Nevertheless, the side chain interactions of the C-terminal tail with the DLG1 GK domain are similar to those of the phosphorylated LGN peptide. Crystal structure of the guanylate kinase domain from discs large homolog 1 (DLG1/SAP97).,Mori S, Tezuka Y, Arakawa A, Handa N, Shirouzu M, Akiyama T, Yokoyama S Biochem Biophys Res Commun. 2013 Jun 7;435(3):334-8. doi:, 10.1016/j.bbrc.2013.04.056. Epub 2013 Apr 25. PMID:23624197[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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