5WY8

Crystal structure of PTP delta Ig1-Ig3 in complex with IL1RAPL1 Ig1-Ig3

Summary for 5WY8

• Entry DOI: 10.2210/pdb5wy8/pdb
• Descriptor: Receptor-type tyrosine-protein phosphatase delta, Interleukin-1 receptor accessory protein-like 1, alpha-L-fucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: synaptic adhesion, hydrolase-protein binding complex, hydrolase/protein binding
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 72767.81

Authors

Kim, H.M.,Won, S.Y.,Kim, D. (deposition date: 2017-01-11, release date: 2017-11-22, Last modification date: 2024-10-16)

Primary citation

Won, S.Y.,Kim, C.Y.,Kim, D.,Ko, J.,Um, J.W.,Lee, S.B.,Buck, M.,Kim, E.,Heo, W.D.,Lee, J.O.,Kim, H.M.
LAR-RPTP Clustering Is Modulated by Competitive Binding between Synaptic Adhesion Partners and Heparan Sulfate
Front Mol Neurosci, 10:327-327, 2017

PubMed Abstract: The leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) are cellular receptors of heparan sulfate (HS) and chondroitin sulfate (CS) proteoglycans that direct axonal growth and neuronal regeneration. LAR-RPTPs are also synaptic adhesion molecules that form -synaptic adhesion complexes by binding to various postsynaptic adhesion ligands, such as Slit- and Trk-like family of proteins (Slitrks), IL-1 receptor accessory protein-like 1 (IL1RAPL1), interleukin-1 receptor accessory protein (IL-1RAcP) and neurotrophin receptor tyrosine kinase C (TrkC), to regulate synaptogenesis. Here, we determined the crystal structure of the human LAR-RPTP/IL1RAPL1 complex and found that lateral interactions between neighboring LAR-RPTP/IL1RAPL1 complexes in crystal lattices are critical for the higher-order assembly and synaptogenic activity of these complexes. Moreover, we found that LAR-RPTP binding to the postsynaptic adhesion ligands, Slitrk3, IL1RAPL1 and IL-1RAcP, but not TrkC, induces reciprocal higher-order clustering of -synaptic adhesion complexes. Although LAR-RPTP clustering was induced by either HS or postsynaptic adhesion ligands, the dominant binding of HS to the LAR-RPTP was capable of dismantling pre-established LAR-RPTP-mediated -synaptic adhesion complexes. These findings collectively suggest that LAR-RPTP clustering for synaptogenesis is modulated by a complex synapse-organizing protein network.

PubMed: 29081732
DOI: 10.3389/fnmol.2017.00327

Experimental method

X-RAY DIFFRACTION (3.07 Å)