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Molecular modeling study about consequences of human β1 adrenoceptor Ser49Gly and Gly389Arg polymorphisms
Author(s) -
CorreaBasurto Jose,
Ciprés Fabiola,
TrujilloFerrara Jose G,
SorianoÚrsua Marvin Antonio
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.769.4
Subject(s) - in silico , glycosylation , chemistry , ligand (biochemistry) , phosphorylation , intracellular , molecular model , extracellular , docking (animal) , computational biology , biophysics , receptor , biology , biochemistry , gene , medicine , nursing
Two human β1 adrenoceptor (Hβ1AR) polymorphisms have been widely studied (Ser49Gly and Gly389Arg). In this study, Hβ1AR 3‐D models with/without these polymorphisms were built and refined. For studying ligand binding process, docking simulations was carried out using a set of known ligands. The binding sites and affinity values on Hβ1AR structures were analyzed. Additionally, glycosylation and phosphorylation were in silico‐evaluated. Results showed differences in ligand Hβ1AR affinity and recognition mode. Besides, conformational disposition of extracellular and intracellular loops was different among structures. The former could be related to differences in glycosylation and phosphorylation processes.