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Article

Mutation of important amino acid residue of Asp104Lys in human beta(1)-adrenergic receptor triggers functional and constitutive inactivation.

Biological & pharmaceutical bulletin - 1 Aug 2008

Hossain Murad, Ahmed Maruf, Bhuiyan Mohiuddin Ahmed, Ishiguro Masaji, Nakamura Takashi, Ozaki Masanobu, Nagatomo Takafumi

Abstract excerpt

Based on our previous molecular modeling and radioligand binding study, we have demonstrated that aspartic acid of 104 in transmembrane helix (TMH) II of beta(1)-adrenergic receptor (beta(1)-AR) is important for functional characteristics of these receptors. We have also showed that mutation of negatively charged aspartic acid to neutral charged alanine exhibited constitutive activity of beta(1)-AR. However, the...

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PMID: 18670082
DOI: 10.1248/bpb.31.1517

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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