5E5R
Crystal structure of the complex between Carbonic anhydrase-like domain of PTPRG and Immunoglobulin domains 2-3 of CNTN3
Summary for 5E5R
| Entry DOI | 10.2210/pdb5e5r/pdb |
| Related | 5E4I 5E4Q 5E4S 5E52 5E53 5E55 5E5U |
| Descriptor | Receptor-type tyrosine-protein phosphatase gamma, Contactin-3, MALONATE ION, ... (5 entities in total) |
| Functional Keywords | neural cell adhesion molecule, receptor-type protein tyrosine phosphatase, immunoglobulin domains, carbonic anhydrase-like domain, hydrolase-cell adhesion complex, hydrolase/cell adhesion |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 104228.49 |
| Authors | Nikolaienko, R.M.,Bouyain, S. (deposition date: 2015-10-09, release date: 2016-08-31, Last modification date: 2024-11-06) |
| Primary citation | Nikolaienko, R.M.,Hammel, M.,Dubreuil, V.,Zalmai, R.,Hall, D.R.,Mehzabeen, N.,Karuppan, S.J.,Harroch, S.,Stella, S.L.,Bouyain, S. Structural Basis for Interactions Between Contactin Family Members and Protein-tyrosine Phosphatase Receptor Type G in Neural Tissues. J.Biol.Chem., 291:21335-21349, 2016 Cited by PubMed Abstract: Protein-tyrosine phosphatase receptor type G (RPTPγ/PTPRG) interacts in vitro with contactin-3-6 (CNTN3-6), a group of glycophosphatidylinositol-anchored cell adhesion molecules involved in the wiring of the nervous system. In addition to PTPRG, CNTNs associate with multiple transmembrane proteins and signal inside the cell via cis-binding partners to alleviate the absence of an intracellular region. Here, we use comprehensive biochemical and structural analyses to demonstrate that PTPRG·CNTN3-6 complexes share similar binding affinities and a conserved arrangement. Furthermore, as a first step to identifying PTPRG·CNTN complexes in vivo, we found that PTPRG and CNTN3 associate in the outer segments of mouse rod photoreceptor cells. In particular, PTPRG and CNTN3 form cis-complexes at the surface of photoreceptors yet interact in trans when expressed on the surfaces of apposing cells. Further structural analyses suggest that all CNTN ectodomains adopt a bent conformation and might lie parallel to the cell surface to accommodate these cis and trans binding modes. Taken together, these studies identify a PTPRG·CNTN complex in vivo and provide novel insights into PTPRG- and CNTN-mediated signaling. PubMed: 27539848DOI: 10.1074/jbc.M116.742163 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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