ArticlePloS one2010
A full pharmacological analysis of the three turkey β-adrenoceptors and comparison with the human β-adrenoceptors.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 30 citations in OpenAlex.
- Biased Signaling and Its Role in the Genesis of Short- and Long-Acting βBiochemistry · 2025Article
- Maximum likelihood estimation under the Emax model: existence, geometry and efficiency.Statistical papers (Berlin, Germany) · 2025Article
- Structures of βNature communications · 2022Article
- Structural basis and mechanism of activation of two different families of G proteins by the same GPCR.Nature structural & molecular biology · 2021Article
- A monoclonal antibody raised against a thermo-stabilised βBiochemical pharmacology · 2018Article
- The βBritish journal of pharmacology · 2017Article
- Ligand occupancy in crystal structure of β1-adrenergic G protein-coupled receptor.Nature structural & molecular biology · 2015Article
- Pharmacological Analysis and Structure Determination of 7-Methylcyanopindolol-Bound β1-Adrenergic Receptor.Molecular pharmacology · 2015Article
- Identification of key residues in transmembrane 4 responsible for the secondary, low-affinity conformation of the human β1-adrenoceptor.Molecular pharmacology · 2014Article
- The Concise Guide to PHARMACOLOGY 2013/14: G protein-coupled receptors.British journal of pharmacology · 2013Article
- Cardiovascular responses to retigabine in conscious rats--under normotensive and hypertensive conditions.British journal of pharmacology · 2013Article
- Comparison of dynamics of extracellular accesses to the β(1) and β(2) adrenoceptors binding sites uncovers the potential of kinetic basis of antagonist selectivity.Chemical biology & drug design · 2012Article
- The pharmacological effects of the thermostabilising (m23) mutations and intra and extracellular (β36) deletions essential for crystallisation of the turkey β-adrenoceptor.Naunyn-Schmiedeberg's archives of pharmacology · 2011Article
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1 author at 1 institution in 1 country.
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Abstract
backgroundThere are three turkey β-adrenoceptors: the original turkey β-adrenoceptor from erythrocytes (tβtrunc, for which the X-ray crystal structure has recently been determined), tβ3C and tβ4C-receptors. This study examined the similarities and differences between these avian receptors and mammalian receptors with regards to binding characteristics and functional high and low affinity agonist conformations. METHODOLOGY/PRINCIPAL
findingsStable cell lines were constructed with each of the turkey β-adrenoceptors and 3H-CGP12177 whole cell binding, CRE-SPAP production and (3)H-cAMP accumulation assays performed. It was confirmed that the three turkey β-adrenoceptors are distinct from each other in terms of amino acid sequence and binding characteristics. The greatest similarity of any of the turkey β-adrenoceptors to human β-adrenoceptors is between the turkey β3C-receptor and the human β2-adrenoceptor. There are pharmacologically distinct differences between the binding of ligands for the tβtrunc and tβ4C and the human β-adrenoceptors (e.g. with CGP20712A and ICI118551). The tβtrunc and tβ4C-adrenoceptors appear to exist in at least two different agonist conformations in a similar manner to that seen at both the human and rat β1-adrenoceptor and human β3-adrenoceptors. The tβ3C-receptor, similar to the human β2-adrenoceptor, does not, at least so far, appear to exist in more than one agonist conformation. CONCLUSIONS/SIGNIFICANCE: There are several similarities, but also several important differences, between the recently crystallised turkey β-adrenoceptor and the human β-adrenoceptors. These findings are important for those the field of drug discovery using the recently structural information from crystallised receptors to aid drug design. Furthermore, comparison of the amino-acid sequence for the turkey and human adrenoceptors may therefore shed more light on the residues involved in the existence of the secondary β-adrenoceptor conformation.
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