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Article

Mutagenesis within helix 6 of the human beta1-adrenergic receptor identifies Lysine324 as a residue involved in imparting the high-affinity binding state of agonists.

Molecular pharmacology - 1 Sept 2006

Zeitoun Omeima, Santos Noel M Delos, Gardner Lidia A, White Stephen W, Bahouth Suleiman W

Abstract excerpt

Competition binding isotherms for agonists to G protein-coupled receptors (GPCR) display high and low binding affinities. Mutagenesis of lysine at position 324 in helix 6 of the wild-type (WT) human beta1-adrenergic receptor (beta1-AR) generated mutant receptors that had GTP-insensitive single low-affinity binding sites for agonists and reduced potencies of full or partial agonists in stimulating adenylyl...

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Share to Adenylyl Cyclases
Share to GTP-Binding Protein alpha Subunits, Gs

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16760361
DOI: 10.1124/mol.106.025346

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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