7OL4
Mouse contactin-1 neurofascin-155 immunoglobulin domains adhesion complex
Summary for 7OL4
| Entry DOI | 10.2210/pdb7ol4/pdb |
| Related | 7OK5 7OL2 |
| Descriptor | Contactin-1, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (14 entities in total) |
| Functional Keywords | heterophilic complex, immunoglobulin cell adhesion protein, neural cell adhesion protein, horseshoe, cell adhesion |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 4 |
| Total formula weight | 287605.79 |
| Authors | Chataigner, L.M.P.,Janssen, B.J.C. (deposition date: 2021-05-19, release date: 2022-12-14, Last modification date: 2024-10-09) |
| Primary citation | Chataigner, L.M.P.,Gogou, C.,den Boer, M.A.,Frias, C.P.,Thies-Weesie, D.M.E.,Granneman, J.C.M.,Heck, A.J.R.,Meijer, D.H.,Janssen, B.J.C. Structural insights into the contactin 1 - neurofascin 155 adhesion complex. Nat Commun, 13:6607-6607, 2022 Cited by PubMed Abstract: Cell-surface expressed contactin 1 and neurofascin 155 control wiring of the nervous system and interact across cells to form and maintain paranodal myelin-axon junctions. The molecular mechanism of contactin 1 - neurofascin 155 adhesion complex formation is unresolved. Crystallographic structures of complexed and individual contactin 1 and neurofascin 155 binding regions presented here, provide a rich picture of how competing and complementary interfaces, post-translational glycosylation, splice differences and structural plasticity enable formation of diverse adhesion sites. Structural, biophysical, and cell-clustering analysis reveal how conserved Ig1-2 interfaces form competing heterophilic contactin 1 - neurofascin 155 and homophilic neurofascin 155 complexes whereas contactin 1 forms low-affinity clusters through interfaces on Ig3-6. The structures explain how the heterophilic Ig1-Ig4 horseshoe's in the contactin 1 - neurofascin 155 complex define the 7.4 nm paranodal spacing and how the remaining six domains enable bridging of distinct intercellular distances. PubMed: 36329006DOI: 10.1038/s41467-022-34302-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.8 Å) |
Structure validation
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