Your browser doesn't support javascript.
loading
ATP binding site on the C-terminus of the vanilloid receptor.
Grycova, Lenka; Lansky, Zdenek; Friedlova, Eliska; Vlachova, Viktorie; Kubala, Martin; Obsilova, Veronika; Obsil, Tomas; Teisinger, Jan.
Afiliação
  • Grycova L; Institute of Physiology, Academy of Sciences of the Czech Republic, Vídenská 1083, 14220 Prague, Czech Republic.
Arch Biochem Biophys ; 465(2): 389-98, 2007 Sep 15.
Article em En | MEDLINE | ID: mdl-17706589
ABSTRACT
Transient receptor potential channel vanilloid receptor subunit 1 (TRPV1) is a thermosensitive cation channel activated by noxious heat as well as a wide range of chemical stimuli. Although ATP by itself does not directly activate TRPV1, it was shown that intracellular ATP increases its activity by directly interacting with the Walker A motif residing on the C-terminus of TRPV1. In order to identify the amino acid residues that are essential for the binding of ATP to the TRPV1 channel, we performed the following point mutations of the Walker A motif P732A, D733A, G734A, K735A, D736A, and D737A. Employing bulk fluorescence measurements, namely a TNP-ATP competition assay and FITC labelling and quenching experiments, we identified the key role of the K735 residue in the binding of the nucleotide. Experimental data was interpreted according to our molecular modelling simulations.
Assuntos
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Modelos Moleculares / Trifosfato de Adenosina / Canais de Cátion TRPV / Modelos Químicos Idioma: En Revista: Arch Biochem Biophys Ano de publicação: 2007 Tipo de documento: Article País de afiliação: República Tcheca
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Modelos Moleculares / Trifosfato de Adenosina / Canais de Cátion TRPV / Modelos Químicos Idioma: En Revista: Arch Biochem Biophys Ano de publicação: 2007 Tipo de documento: Article País de afiliação: República Tcheca