3W9Y

Crystal structure of the human DLG1 guanylate kinase domain

Summary for 3W9Y

• Entry DOI: 10.2210/pdb3w9y/pdb
• Descriptor: Disks large homolog 1 (2 entities in total)
• Functional Keywords: guanylate kinase, molecular scaffold, peptide binding, cell membrane, peptide binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 23404.50

Authors

Mori, S.,Tezuka, Y.,Arakawa, A.,Handa, N.,Shirouzu, M.,Akiyama, T.,Yokoyama, S. (deposition date: 2013-04-18, release date: 2013-06-26, Last modification date: 2024-11-06)

Primary citation

Mori, S.,Tezuka, Y.,Arakawa, A.,Handa, N.,Shirouzu, M.,Akiyama, T.,Yokoyama, S.
Crystal structure of the guanylate kinase domain from discs large homolog 1 (DLG1/SAP97)
Biochem.Biophys.Res.Commun., 435:334-338, 2013

PubMed Abstract: 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.

PubMed: 23624197
DOI: 10.1016/j.bbrc.2013.04.056

Experimental method

X-RAY DIFFRACTION (2.2 Å)