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Binding of the neuroleptic drug haloperidol to a monoclonal antibody: Refinement of the binding site molecular model using canonical structures
Author(s) -
Anchin Jerry M.,
Subramaniam Shankar,
Linthicum D. Scott
Publication year - 1991
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300040103
Subject(s) - binding site , haloperidol , chemistry , monoclonal antibody , stacking , ligand (biochemistry) , stereochemistry , molecular model , hydrogen bond , drug , docking (animal) , computational biology , combinatorial chemistry , antibody , biochemistry , biology , genetics , pharmacology , receptor , molecule , medicine , organic chemistry , neuroscience , dopamine , nursing
The ligand binding site of a monoclonal antibody (185), which binds the neuroleptic drug haloperidol, has been modelled using canonical structures and energy minimization techniques. This refined modelling protocol has allowed us to predict the variable region loop conformation. Three key residues, H:50(W), H:100a(D) and L:96(Y) appear to create the basis of the electrostatic, π–π stacking interactions and hydrogen bonding required for the high affinity binding site characteristics present in this antibody. The use of computer‐aided graphics techniques and appropriate three‐dimensional modelling permits inspection of the predicted molecular recognition features of the ligand binding site.