1989
DOI: 10.1016/0014-5793(89)80276-5
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Chemical characterization of ligand binding site fragments from turkey β‐adrenergic receptor

Abstract: Affinity-labeled ~-adrenergic receptor from turkey erythrocyte membranes was specifically cleaved near cysteine residues after S-cyanylation. Analysis of the labeled polypeptide fragments suggests that iodocyanopindolol diazirine reacted with an amino acid residue which is located in the non-glycosylated region containing the sixth and seventh transmembrane domains of the receptor. However, the possibility cannot be excluded that a second residue, located between the third and fifth transmembrane domains, was … Show more

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Cited by 3 publications
(3 citation statements)
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“…The approach involving covalent labelling with specific ligands has provided structural information for adrenergic (Dohlman et al, 1988;Wong et al, 1988;Eshdat et al, 1989;Matsui et al, 1989;Strader et al, 1989) or muscarinic cholinergic (Curtis et al, 1989; Hulme et al, 1989) receptors. Examples of topography of peptide-hormone interaction with their receptors have not yet been reported.…”
Section: Discussionmentioning
confidence: 99%
“…The approach involving covalent labelling with specific ligands has provided structural information for adrenergic (Dohlman et al, 1988;Wong et al, 1988;Eshdat et al, 1989;Matsui et al, 1989;Strader et al, 1989) or muscarinic cholinergic (Curtis et al, 1989; Hulme et al, 1989) receptors. Examples of topography of peptide-hormone interaction with their receptors have not yet been reported.…”
Section: Discussionmentioning
confidence: 99%
“…2. lane b). Due to the nature of the affinity label and data from previous studies in which this reagent was used (Dohlman et al, 1987;Eshdat et al, 1989), this reagent was not expected to bind covalently to a region overlapping with the peptides used for immunization. Indeed, the ligand-binding domain of the receptor is formed by a pocket of hydrophobic transmembrane helices, whereas potential immunogenic peptides were selected from hydrophilic parts of the protein.…”
Section: Immunoprecipitation Assaymentioning
confidence: 99%
“…In those studies the disulfide bond was easily reduced in the presence of DTT. Similarly, hydroxylamine readily cleaves ester groups, and its ability to remove an affinity label from a fragment of the /3-adrenergic receptor fragment was interpreted to indicate an ester linkage (22).…”
Section: Discussionmentioning
confidence: 99%