7OL2

Crystal structure of mouse contactin 1 immunoglobulin domains

Summary for 7OL2

• Entry DOI: 10.2210/pdb7ol2/pdb
• 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, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: zipper, dimer, glycoprotein, immunoglobulin cell adhesion protein neural cell adhesion protein, horseshoe, cell adhesion
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 2
• Total formula weight: 139513.47

Authors

Chataigner, L.M.P.,Janssen, B.J.C. (deposition date: 2021-05-19, release date: 2022-12-14, Last modification date: 2024-11-13)

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

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: 36329006
DOI: 10.1038/s41467-022-34302-9

Experimental method

X-RAY DIFFRACTION (3.89 Å)