Conformational flexibility of three cytoplasmic segments of the angiotensin II AT(1A) receptor: A circular dichroism and fluorescence spectroscopy study

Conformational flexibility of three cytoplasmic segments of the angiotensin II AT(1A) receptor: A circular dichroism and fluorescence spectroscopy study

Autor Pertinhez, Thelma A. Google Scholar
Krybus, Regina Google Scholar
Cilli, Eduardo Maffud Autor UNIFESP Google Scholar
Paiva, Antonio Cechelli de Mattos Autor UNIFESP Google Scholar
Nakaie, Clovis Ryuichi Autor UNIFESP Google Scholar
Franzoni, Lorella Google Scholar
Sartor, Giorgio Google Scholar
Spisni, Alberto Google Scholar
Schreier, Shirley Google Scholar
Instituição Univ Parma
LNLS
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Resumo The conformation of three synthetic peptides encompassing the proximal and distal half of the third intracellular loop (Ni3 and Ci3) and a portion of the cytoplasmic tail (fCT) of the angiotensin II AT(1A) receptor has been studied using circular dischroism and fluorescence spectroscopies. the results show that the conformation of the peptides is modulated in various ways by the environmental conditions (pH, ionic strength and dielectric constant). Indeed, Ni3 and fCT fold into helical structures that possess distinct stability and polarity due to the diverse forces involved: mainly polar interactions in the first case and a combination of polar and hydrophobic interactions in the second. the presence of these various features also produce distinct intermolecular interactions. Ci3, instead, exists as an ensemble of partially folded states in equilibrium. Since the corresponding regions of the angiotensin II AT(1A) receptor are known to play an important role in the receptor function, due to their ability to undergo conformational changes, these data provide some new clues about their different conformational plasticity. Copyright (C) 2002 European Peptide Society and John Wiley Sons, Ltd.
Assunto angiotensin II AT(1A) receptor
circular dichroism
fluorescence
G-protein
Idioma Inglês
Data 2002-01-01
Publicado em Journal of Peptide Science. W Sussex: John Wiley & Sons Ltd, v. 8, n. 1, p. 23-35, 2002.
ISSN 1075-2617 (Sherpa/Romeo, fator de impacto)
Editor Wiley-Blackwell
Extensão 23-35
Fonte http://dx.doi.org/10.1002/psc.364
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000173575400004
URI http://repositorio.unifesp.br/handle/11600/26694

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