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Crystal structure of the guanylate kinase domain from discs large homolog 1 (DLG1/SAP97).
|Title||Crystal structure of the guanylate kinase domain from discs large homolog 1 (DLG1/SAP97).|
|Publication Type||Journal Article|
|Year of Publication||2013|
|Authors||Mori S, Tezuka Y, Arakawa A, Handa N, Shirouzu M, Akiyama T, Yokoyama S|
|Journal||Biochemical and biophysical research communications|
|Date Published||2013 Jun 7|
Discs 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.
|Alternate Journal||Biochem. Biophys. Res. Commun.|