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Substrate recognition mechanism of human beta-adrenergic receptor kinase 1 based on a three-dimensional model structure

Iino, M.; Shibano, T.

Drug Design and Discovery 14(2): 145-155

1996


ISSN/ISBN: 1055-9612
PMID: 9010620
Accession: 047474001

Although its detailed substrate specificity is not precisely known, beta-adrenergic receptor kinase 1 phosphorylates beta 2-adrenergic receptors and other G protein-coupled receptors. To elucidate the ligand recognition mechanism of the enzyme and the consensus sequence required for substrates, a three-dimensional structure of the catalytic domain of the enzyme was modeled based on the X-ray crystal structure of the catalytic subunit of cyclic AMP-dependent protein kinase A. When the phosphorylation residue of the substrate was defined as the p position in the model of beta-adrenergic receptor kinase 1, the present study suggested that the consensus sequence recognized by this enzyme would consist of a basic residue at p-3 and an acidic residue at p-2.

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