8A0Y
Crystal structure of mouse contactin 2 immunoglobulin domains
Summary for 8A0Y
| Entry DOI | 10.2210/pdb8a0y/pdb |
| Related | 1CS6 2OM5 |
| Descriptor | Contactin-2, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| Functional Keywords | cell adhesion molecule(s), immunoglobulin, glycoprotein, myelin, juxtaparanodal, contactin, tag-1, axonin-1, tax-1, horseshoe, cell adhesion |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 3 |
| Total formula weight | 202967.41 |
| Authors | Chataigner, L.M.P.,Janssen, B.J.C. (deposition date: 2022-05-30, release date: 2023-11-01, Last modification date: 2024-11-06) |
| Primary citation | Chataigner, L.M.P.,Tharichen, L.,Beugelink, J.W.,Granneman, J.C.M.,Mokiem, N.J.,Snijder, J.,Forster, F.,Janssen, B.J.C. Contactin 2 homophilic adhesion structure and conformational plasticity. Structure, 32:60-, 2024 Cited by PubMed Abstract: 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 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 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. PubMed: 37992710DOI: 10.1016/j.str.2023.10.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
Download full validation report
