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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