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5E53

Crystal structure of chicken CNTN1 FN1-FN3 domains

Summary for 5E53
Entry DOI10.2210/pdb5e53/pdb
Related5E4I 5E4Q 5E4S 5E52 5E55
DescriptorContactin-1, IMIDAZOLE (3 entities in total)
Functional Keywordsneural cell adhesion molecule, fibronectin type iii domains, cell adhesion
Biological sourceGallus gallus (Chicken)
Total number of polymer chains4
Total formula weight135237.43
Authors
Nikolaienko, R.M.,Bouyain, S. (deposition date: 2015-10-07, release date: 2016-08-31, Last modification date: 2023-09-27)
Primary citationNikolaienko, 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: 27539848
DOI: 10.1074/jbc.M116.742163
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.497 Å)
Structure validation

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数据于2024-11-06公开中

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