Functionally different agonists induce distinct conformations in the G protein coupling domain of the beta 2 adrenergic receptor.

Ghanouni, P; Gryczynski, Z; Steenhuis, J J; Lee, T W; Farrens, D L; Lakowicz, J R; Kobilka, B K

Ghanouni, P; Gryczynski, Z; Steenhuis, J J; Lee, T W; Farrens, D L; Lakowicz, J R; Kobilka, B K.

Affiliation

Ghanouni P; Department of Molecular and Cellular Physiology and Division of Cardiovascular Medicine, Howard Hughes Medical Institute, Stanford University Medical School, Stanford, CA 94305, USA.

J Biol Chem ; 276(27): 24433-6, 2001 Jul 06.

Article in En | MEDLINE | ID: mdl-11320077

Subject(s)

Adrenergic beta-Agonists/metabolism; GTP-Binding Proteins/metabolism; Receptors, Adrenergic, beta-2/metabolism; Adrenergic beta-Agonists/chemistry; Fluoresceins; Isoproterenol/metabolism; Ligands; Protein Binding; Protein Conformation; Receptors, Adrenergic, beta-2/chemistry; Spectrometry, Fluorescence; Structure-Activity Relationship

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Collection: 01-internacional Database: MEDLINE Main subject: Receptors, Adrenergic, beta-2 / Adrenergic beta-Agonists / GTP-Binding Proteins Language: En Journal: J Biol Chem Year: 2001 Document type: Article Affiliation country: United States Country of publication: United States

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