Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor

Autores Principales: Baier, Carlos J., Fantini, Jacques , Barrantes, Francisco J.
Formato: Artículo
Lenguaje: English
Publicado: 2011
Materias:
Acceso en línea: http://bibliotecadigital.uca.edu.ar/repositorio/investigacion/disclosure-cholesterol-recognition-motifs.pdf
building BDUCA
institution Biblioteca Digital (UCA)
id BDUCA--investigacion:disclosure-cholesterol-recognition-motifs
author Baier, Carlos J.
Fantini, Jacques
Barrantes, Francisco J.
spellingShingle Baier, Carlos J.
Fantini, Jacques
Barrantes, Francisco J.
COLESTEROL
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
Abstract: Cholesterol influences ion-channel function, distribution and clustering in the membrane, endocytosis, and exocytic sorting of the nicotinic acetylcholine receptor (AChR). We report the occurrence of a cholesterol recognition motif, here coined ‘‘CARC’’, in the transmembrane regions of AChR subunits that bear extensive contact with the surrounding lipid, and are thus optimally suited to convey cholesterol-mediated signaling from the latter. Three cholesterol molecules could be docked on the transmembrane segments of each AChR subunit, rendering a total of 15 cholesterol molecules per AChR molecule. The CARC motifs contribute each with an energy of interaction between 35 and 52 kJ.mol21, adding up to a total of about 200 kJ.mol21 per receptor molecule, i.e. 40% of the lipid solvation free energy/ AChR molecule. The CARC motif is remarkably conserved along the phylogenetic scale, from prokaryotes to human, suggesting that it could be responsible for some of the above structural/functional properties of the AChR.
topic COLESTEROL
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
topic_facet COLESTEROL
LIPIDOS
CANALES IONICOS
NEUROCIENCIA
ACHR
NEUROBIOLOGIA MOLECULAR
title Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_full Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_fullStr Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_full_unstemmed Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
title_short Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
contents Abstract: Cholesterol influences ion-channel function, distribution and clustering in the membrane, endocytosis, and exocytic sorting of the nicotinic acetylcholine receptor (AChR). We report the occurrence of a cholesterol recognition motif, here coined ‘‘CARC’’, in the transmembrane regions of AChR subunits that bear extensive contact with the surrounding lipid, and are thus optimally suited to convey cholesterol-mediated signaling from the latter. Three cholesterol molecules could be docked on the transmembrane segments of each AChR subunit, rendering a total of 15 cholesterol molecules per AChR molecule. The CARC motifs contribute each with an energy of interaction between 35 and 52 kJ.mol21, adding up to a total of about 200 kJ.mol21 per receptor molecule, i.e. 40% of the lipid solvation free energy/ AChR molecule. The CARC motif is remarkably conserved along the phylogenetic scale, from prokaryotes to human, suggesting that it could be responsible for some of the above structural/functional properties of the AChR.
url http://bibliotecadigital.uca.edu.ar/repositorio/investigacion/disclosure-cholesterol-recognition-motifs.pdf
format Artículo
genre Artículo
genre_facet Artículo
era 2011
era_facet 2011
publishDate 2011
language English
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score 12,758687