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. Author manuscript; available in PMC: 2024 Aug 1.
Published in final edited form as: J Immunol. 2023 Aug 1;211(3):343–349. doi: 10.4049/jimmunol.2300098

Figure 2: Regulating classical cadherin adhesion.

Figure 2:

Cadherin adhesion can be regulating either via extracellular binding with antibodies or from the inside-out by cytoplasmic proteins. Activating antibodies 19A11 (magenta, PDB: 6CXY) and 66E8 (cyan, PDB:6VEL) recognize E-cadherin EC1 or EC2 domain (green, PDB: 3Q2V) near the cadherin trans binding sites. Antibody TSP7 (blue, PDB: 5JYL) inhibits P-cadherin adhesion by binding on the EC1 domain while 67G8 (orange) inhibits E-cadherin adhesion by binding on EC5 domain. The intracellular domain of cadherin (green) associates with various signaling molecules, including β-catenin (pink, PDB: 3L6X), p120-catenin (light yellow, PDB: 4R10), α-catenin (red), and vinculin (grey), which eventually link the cadherin cytoplasmic region to F-actin. The structures of α-catenin, vinculin, and E-cadherin intracellular domain were predicted using Alphafold (94). Unless apparent from the crystal structure, all interactions were predicted using Alphafold.