Hi everyone, I'm working on structure of an antibody that inhibits a receptor. The antibody doesn't induce any conformational change in the receptor and doesn't bind the ligand binding site. If we superimpose the receptor with antibody and ligand the only hindrance we find is a electrostatic repulsion between two arginines (3.3A): one is part of the antibody and one is part of the ligand and involved in ligand binding. However the arginine coming from the antibody makes a salt bridge with an aspartic acid from the receptor. Does this neutralize it's charge? Can we still say that it has a repulsive effect? Thanks
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