5XWS
Crystal structure of SALM5 LRR-Ig
Summary for 5XWS
| Entry DOI | 10.2210/pdb5xws/pdb |
| Descriptor | Leucine-rich repeat and fibronectin type-III domain-containing protein 5, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | synaptic orgnizers, cell adhesion |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 41807.90 |
| Authors | Goto-Ito, S.,Yamagata, A.,Sato, Y.,Fukai, S. (deposition date: 2017-06-30, release date: 2018-06-06, Last modification date: 2020-07-29) |
| 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 Cited by 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: 29348429DOI: 10.1038/s41467-017-02417-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.084 Å) |
Structure validation
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