Please use this identifier to cite or link to this item: https://repositorio.uca.edu.ar/handle/123456789/1462
Título : Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor
Autor : Baier, Carlos J. 
Fantini, Jacques 
Barrantes, Francisco José 
Palabras clave : COLESTEROLLIPIDOSCANALES IONICOSNEUROCIENCIAACHRNEUROBIOLOGIA MOLECULAR
Fecha de publicación : 2011
Editorial : Nature Research
Cita : Baier, C. J., Fantini, J., Barrantes, F. J. Disclosure of cholsterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor [en línea]. Scientific Reports. 2011. 1 (69). doi:10.1038/srep00069. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/1462
Resumen : 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.
URI : https://repositorio.uca.edu.ar/handle/123456789/1462
ISSN : 2045-2322
Disciplina: MEDICINA
DOI: 10.1038/srep00069
Derechos: Acceso Abierto
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