5B64

A novel binding mode of MAGUK GK domain revealed by DLG GK domain in complex with KIF13B MBS domain

Summary for 5B64

• Entry DOI: 10.2210/pdb5b64/pdb
• Descriptor: DLG GK, Protein Kif13b, SULFATE ION, ... (5 entities in total)
• Functional Keywords: maguk, gk, kif13b, mbs, kinesin, motor, peptide binding protein
• Biological source: Rattus; More
• Total number of polymer chains: 2
• Total formula weight: 37176.57

Authors

Shang, Y.,Zhu, J.,Zhang, M. (deposition date: 2016-05-24, release date: 2016-10-12, Last modification date: 2024-03-20)

Primary citation

Zhu, J.,Shang, Y.,Xia, Y.,Zhang, R.,Zhang, M.
An Atypical MAGUK GK Target Recognition Mode Revealed by the Interaction between DLG and KIF13B
Structure, 24:1876-1885, 2016

PubMed Abstract: The membrane-associated guanylate kinase (MAGUK) scaffold proteins share a signature guanylate kinase (GK) domain. Despite their diverse functional roles in cell polarity control and synaptic signaling, the currently known mode of action of MAGUK GK is via its binding to phosphorylated short peptides from target proteins. Here, we discover that the GK domain of DLG MAGUK binds to an unphosphorylated and autonomously folded domain within the stalk region (MAGUK binding stalk [MBS] domain) of a kinesin motor KIF13B with high specificity and affinity. The structure of DLG4 GK in complex with KIF13B MBS reveals the molecular mechanism governing this atypical GK/target recognition mode and provides insights into DLG/KIF13B complex-mediated regulation of diverse cellular processes such as asymmetric cell division. We further show that binding to non-phosphorylated targets is another general property of MAGUK GKs, thus expanding the mechanisms of action of the MAGUK family proteins.

PubMed: 27642159
DOI: 10.1016/j.str.2016.08.008

Experimental method

X-RAY DIFFRACTION (2.7 Å)