5e5u

Crystal structure of the complex between Carbonic anhydrase-like domain of PTPRG and Immunoglobulin domains 2-3 of CNTN6

spinqualitylabelsall models 5e5u, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5e5u is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PS, ACY, FMT, MLI, MLT Related: 5e4q, 5e4i, 5e4s, 5e52, 5e53, 5e55, 5e5r Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PTPRG_MOUSE] Possesses tyrosine phosphatase activity (By similarity). [CNTN6_MOUSE] Contactins mediate cell surface interactions during nervous system development. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus (By similarity). Involved in motor coordination. Publication Abstract from PubMed Protein tyrosine phosphatase receptor type G (RPTPgamma/PTPRG) interacts in vitro with contactin-3-6 (CNTN3-6), a group of glycosylphosphatidyl-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[middot]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. Structural Basis for Interactions Between Contactin Family Members and Protein Tyrosine Phosphatase Receptor Type G in Neural Tissues.,Nikolaienko RM, Hammel M, Dubreuil V, Zalmai R, Hall DR, Mehzabeen N, Karuppan SJ, Harroch S, Stella SL, Bouyain S J Biol Chem. 2016 Aug 18. pii: jbc.M116.742163. PMID:27539848 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Contactin

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