Homophilic vs.

<p><b>Heterophilic Ig-Horseshoe Zipper interface. A) Contactin-2 Homophilic dimer interface</b> (PDBid 8a0y). Contactin-2 extracellular region contains 6 N-terminal Ig domains followed by 4 FN3 domains. The four N-terminus Ig-domains Ig1-4) form the Ig-Horseshoe. The Ig2 domain for...

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محفوظ في:
التفاصيل البيبلوغرافية
المؤلف الرئيسي: Caesar Tawfeeq (21087272) (author)
مؤلفون آخرون: Jiyao Wang (2121157) (author), Umesh Khaniya (8822018) (author), Thomas Madej (185877) (author), James Song (4570324) (author), Ravinder Abrol (1425607) (author), Philippe Youkharibache (266279) (author)
منشور في: 2025
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الملخص:<p><b>Heterophilic Ig-Horseshoe Zipper interface. A) Contactin-2 Homophilic dimer interface</b> (PDBid 8a0y). Contactin-2 extracellular region contains 6 N-terminal Ig domains followed by 4 FN3 domains. The four N-terminus Ig-domains Ig1-4) form the Ig-Horseshoe. The Ig2 domain forms a dimer through a G-strand antiparallel zipper interface. <b>B) Contactin-2 Homophilic Horseshoe Zipper interactome</b> showing the G-strand zipper (red) as well as residues in the F and C strands of the GFCC’ sheet <b>C) Contactin-1 - neurofascin-155 Heterophilic dimer interface</b> (PDBid 7OL4). Contactin-1 is highly homologous to Contactin-2 and interacts with <b>neurofascin-155. Both interact through</b> their N-terminal Ig-Horseshoe substructure, also using the Ig2 domain forming a G-strand antiparallel zipper interface. The dimer complexes show nonetheless significant plasticity <a href="https://structure.ncbi.nlm.nih.gov/icn3d/share.html?ZnVaH3FLKjYL4Eod8&t=7OL4,8A0Y" target="_blank">https://structure.ncbi.nlm.nih.gov/icn3d/share.html?ZnVaH3FLKjYL4Eod8&t=7OL4,8A0Y</a><b>. D) Contactin-1 - neurofascin-155 Heterophilic Horseshoe Zipper interactome</b> showing the G-strand zipper (red) as well as residues in the F, C and C strands of the GFCC’ sheet. <b>E) Conserved positional interaction.</b> The G-strand zipper interface is conserved in terms of its positional residue network. However One should note that this does not mean that all the atom level residue interactions are the same. For example while the symmetric pair igs# 9547-9547 involves a conserved antiparallel backbone-backbone interaction in both the homophilic (S9547-S9547) or heterophilic (S9547-I9547) pair, the symmetric pair T9545-F9549 in the homophilic dimer (PDBid 8A0Y) forms a side chain(T)-backbone(F) HBond, replaced in the heterophilic dimer (PDBid 7OL4) by a backbone-backbone HBond in the T9545-Q9549 pair while the pseudo symmetric H9545-F9549 pair is reduced to a vdW interaction.</p>