Crystal structure of the guanylate kinase domain from discs large homolog 1 (DLG1/SAP97)

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• 作者：Shinji Mori^a ; ^b ; Yuta Tezuka^a ; ^c ; Akihiko Arakawa^a ; ^b ; Noriko Handa^b ; Mikako Shirouzu^b ; Tetsu Akiyama^c ; Shigeyuki Yokoyama^a ; ^b ; ^{yokoyama@riken.jp}
• 关键词：GK ; guanylate kinase ; MAGUK ; membrane associated guanylate kinase ; DLG1 ; discs large homolog 1 ; SAP97 ; synapse-associated protein 97 ; p-LGN ; phosphorylated LGN.
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2013
• 出版时间：7 June, 2013
• 年：2013
• 卷：435
• 期：3
• 页码：334-338
• 全文大小：1218 K

文摘

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.