Mutagenesis of the AT(1) receptor reveals different binding modes of angiotensin II and [Sar(1)]-angiotensin II

Mutagenesis of the AT(1) receptor reveals different binding modes of angiotensin II and [Sar(1)]-angiotensin II

Autor Santos, E. L. Google Scholar
Pesquero, J. B. Google Scholar
Oliveira, L. Google Scholar
Paiva, ACM Google Scholar
Costa-Neto, C. M. Google Scholar
Instituição Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Resumo Homology modeling of the structure of the AT, receptor, based on the high resolution rhodopsin crystal structure, indicated that it is unlikely that the binding of AngII to AT(1) involves simultaneously all the receptor's residues reported in the literature to participate in this process. Site-directed mutagenesis using Ala substitution of charged residues Lys(20), Arg(23), Glu(91) and Arg(93) was performed to evaluate the participation of their side-chains in ligand binding and in triggering the cell's response. A comparative analysis by competition binding and functional assays using angiotensin II and the analog [Sar(1)]-angiotensin II suggests an important role for Arg(23) of AT(1) receptor in binding of the natural agonist. It is discussed whether some receptor's residues participate directly in the binding with AngII or whether they are part of a regulatory site. (C) 2004 Elsevier B.V. All rights reserved.
Assunto site-directed mutagenesis
G-protein coupled receptors
Idioma Inglês
Data 2004-07-15
Publicado em Regulatory Peptides. Amsterdam: Elsevier B.V., v. 119, n. 3, p. 183-188, 2004.
ISSN 0167-0115 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 183-188
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000221584100006

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