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Theoretical evidence of a salt bridge disruption as the initiating process for the α 1d ‐adrenergic receptor activation: A molecular dynamics and docking study
Author(s) -
Carrieri A.,
Centeno N.B.,
Rodrigo J.,
Sanz F.,
Carotti A.
Publication year - 2001
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.1051
Subject(s) - docking (animal) , rhodopsin , receptor , salt bridge , molecular dynamics , biophysics , chemistry , computational biology , mutagenesis , molecular model , biology , biochemistry , mutant , computational chemistry , medicine , gene , retinal , nursing
This study reports the building of the three‐dimensional structure of the rat α 1d ‐adrenergic receptor through a topology approach based on the structure of the rhodopsin receptor from cryoelectron microscopy. The validity and reliability of the receptor model were assessed through exhaustive molecular dynamics and docking studies. Some interesting ligand‐receptor interactions were identified along with significant differences between the binding mode of agonists and antagonists. The importance of the disruption of a salt bridge as a possible initial event leading to receptor activation is discussed on the basis of data from mutagenesis and molecular dynamics studies. Proteins 2001;43:382–394. © 2001 Wiley‐Liss, Inc.