Regulation of Beta-2-Adrenergic Receptor Function by Conformationally Selective Single- domain Intrabodies
نویسندگان
چکیده
Department of Medicine, Duke University Medical Center, Durham, North Carolina, 27710, USA (D.P.S., L.M.W., R.T.S., S.A., R.J.L.); Department of Neuroscience and Pharmacology, The Panum Institute, University of Copenhagen, Copenhagen, Denmark (S.G.F.R.); Department of Molecular and Cellular Interactions, Vlaams Instituut voor Biotechnologie (VIB) & Structural Biology, Brussels, Belgium. (E.P., J.S.); Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California, USA, 94305, USA (B.K.K.); Department of Biochemistry, Duke University Medical Center Durham, North Carolina 27710, USA (R.J.L.); Howard Hughes Medical Institute. Duke University Medical Center, Durham, North Carolina 27710, USA (R.J.L.) Molecular Pharmacology Fast Forward. Published on December 6, 2013 as doi:10.1124/mol.113.089516
منابع مشابه
Regulation of b2-Adrenergic Receptor Function by Conformationally Selective Single-Domain Intrabodies s
The biologic activity induced by ligand binding to orthosteric or allosteric sites on a G protein–coupled receptor (GPCR) is mediated by stabilization of specific receptor conformations. In the case of the b2 adrenergic receptor, these ligands are generally small-molecule agonists or antagonists. However, amonomeric single-domain antibody (nanobody) from the Camelid family was recently found to...
متن کاملRegulation of β2-adrenergic receptor function by conformationally selective single-domain intrabodies.
The biologic activity induced by ligand binding to orthosteric or allosteric sites on a G protein-coupled receptor (GPCR) is mediated by stabilization of specific receptor conformations. In the case of the β2 adrenergic receptor, these ligands are generally small-molecule agonists or antagonists. However, a monomeric single-domain antibody (nanobody) from the Camelid family was recently found t...
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تاریخ انتشار 2013