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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CNTN2_MOUSE CNTN2_MOUSE] In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region. | [https://www.uniprot.org/uniprot/CNTN2_MOUSE CNTN2_MOUSE] In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region. | ||
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== Publication Abstract from PubMed == | |||
The cell-surface attached glycoprotein contactin 2 is ubiquitously expressed in the nervous system and mediates homotypic cell-cell interactions to organize cell guidance, differentiation, and adhesion. Contactin 2 consists of six Ig and four fibronectin type III domains (FnIII) of which the first four Ig domains form a horseshoe structure important for homodimerization and oligomerization. Here we report the crystal structure of the six-domain contactin 2(Ig1-6) and show that the Ig5-Ig6 combination is oriented away from the horseshoe with flexion in interdomain connections. Two distinct dimer states, through Ig1-Ig2 and Ig3-Ig6 interactions, together allow formation of larger oligomers. Combined size exclusion chromatography with multiangle light scattering (SEC-MALS), small-angle X-ray scattering (SAXS) and native MS analysis indicates contactin 2(Ig1-6) oligomerizes in a glycan dependent manner. SAXS and negative-stain electron microscopy reveals inherent plasticity of the contactin 2 full-ectodomain. The combination of intermolecular binding sites and ectodomain plasticity explains how contactin 2 can function as a homotypic adhesion molecule in diverse intercellular environments. | |||
Contactin 2 homophilic adhesion structure and conformational plasticity.,Chataigner LMP, Tharichen L, Beugelink JW, Granneman JCM, Mokiem NJ, Snijder J, Forster F, Janssen BJC Structure. 2024 Jan 4;32(1):60-73.e5. doi: 10.1016/j.str.2023.10.012. Epub 2023 , Nov 21. PMID:37992710<ref>PMID:37992710</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||