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Article

Mutations of Tyr326 in the beta 2-adrenoceptor disrupt multiple receptor functions.

European journal of pharmacology - 27 Jun 1996

Gabilondo A M, Krasel C, Lohse M J

Abstract excerpt

A tyrosine residue at the cytoplasmic end of the seventh transmembrane helix is conserved in many G-protein-coupled receptors. In the human beta 2-adrenoceptor, this tyrosine (Tyr326) has been proposed to be a specific determinant for agonist-induced receptor sequestration. In order to probe its contribution to the sequestration process we have replaced this tyrosine by alanine (Y326A) or phenylalanine (Y326F)....

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Identifiers

PMID: 8832227
DOI: 10.1016/0014-2999(96)00247-6

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Related research

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Mutations of Tyr326 in the beta 2-adrenoceptor disrupt multiple receptor functions.PMID 8832227Read ↗

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A Four Amino Acid Deletion Polymorphism in the Third Intracellular Loop of the Human α2C-Adrenergic Receptor Confers Impaired Coupling to Multiple EffectorsSemantic proximity Read ↗

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A proline-rich region of the third intracellular loop imparts phenotypic beta 1-versus beta 2-adrenergic receptor coupling and sequestration.Semantic proximity Read ↗

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