5I99

Crystal structure of mouse CNTN3 Ig5-Fn2 domains

5I99 の概要

• エントリーDOI: 10.2210/pdb5i99/pdb
• 分子名称: Contactin-3, GLYCEROL (3 entities in total)
• 機能のキーワード: neural cell adhesion molecule, immunoglobulin-like domains, fibronectin type iii domains, cell adhesion
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43220.54

構造登録者

Nikolaienko, R.M.,Bouyain, S. (登録日: 2016-02-19, 公開日: 2016-08-31, 最終更新日: 2023-09-27)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2.4 Å)