Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/27839
Title: Mutagenesis of the AT(1) receptor reveals different binding modes of angiotensin II and [Sar(1)]-angiotensin II
Authors: Santos, E. L.
Pesquero, J. B.
Oliveira, L.
Paiva, ACM
Costa-Neto, C. M.
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Keywords: site-directed mutagenesis
modeling
G-protein coupled receptors
sarcosine
Issue Date: 15-Jul-2004
Publisher: Elsevier B.V.
Citation: Regulatory Peptides. Amsterdam: Elsevier B.V., v. 119, n. 3, p. 183-188, 2004.
Abstract: 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.
URI: http://repositorio.unifesp.br/handle/11600/27839
ISSN: 0167-0115
Other Identifiers: http://dx.doi.org/10.1016/j.regpep.2004.02.009
Appears in Collections:Artigo

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.