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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 : | COLESTEROL; LIPIDOS; CANALES IONICOS; NEUROCIENCIA; ACHR; NEUROBIOLOGIA 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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