5XWU

Crystal structure of PTPdelta Ig1-Ig3 in complex with SALM2 LRR-Ig

Summary for 5XWU

• Entry DOI: 10.2210/pdb5xwu/pdb
• Descriptor: Receptor-type tyrosine-protein phosphatase delta, Leucine-rich repeat and fibronectin type III domain-containing protein 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: synaptic orgnizers, cell adhesion
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 4
• Total formula weight: 151924.35

Authors

Goto-Ito, S.,Yamagata, A.,Sato, Y.,Fukai, S. (deposition date: 2017-06-30, release date: 2018-06-06, Last modification date: 2024-10-23)

Primary citation

Goto-Ito, S.,Yamagata, A.,Sato, Y.,Uemura, T.,Shiroshima, T.,Maeda, A.,Imai, A.,Mori, H.,Yoshida, T.,Fukai, S.
Structural basis of trans-synaptic interactions between PTP delta and SALMs for inducing synapse formation.
Nat Commun, 9:269-269, 2018

PubMed Abstract: Synapse formation is triggered by trans-synaptic interactions of cell adhesion molecules, termed synaptic organizers. Three members of type-II receptor protein tyrosine phosphatases (classified as type-IIa RPTPs; PTPδ, PTPσ and LAR) are known as presynaptic organizers. Synaptic adhesion-like molecules (SALMs) have recently emerged as a family of postsynaptic organizers. Although all five SALM isoforms can bind to the type-IIa RPTPs, only SALM3 and SALM5 reportedly have synaptogenic activities depending on their binding. Here, we report the crystal structures of apo-SALM5, and PTPδ-SALM2 and PTPδ-SALM5 complexes. The leucine-rich repeat (LRR) domains of SALMs interact with the second immunoglobulin-like (Ig) domain of PTPδ, whereas the Ig domains of SALMs interact with both the second and third Ig domains of PTPδ. Unexpectedly, the structures exhibit the LRR-mediated 2:2 complex. Our synaptogenic co-culture assay using site-directed SALM5 mutants demonstrates that presynaptic differentiation induced by PTPδ-SALM5 requires the dimeric property of SALM5.

PubMed: 29348429
DOI: 10.1038/s41467-017-02417-z

Experimental method

X-RAY DIFFRACTION (3.162 Å)