Please use this identifier to cite or link to this item: https://repositorio.uca.edu.ar/handle/123456789/1460
Título : Relevance of CARC and CRAC cholesterol-recognition motifs in the nicotinic azcetylcholine receptor and other membrane-bound receptors
Autor : Di Scala, Coralie 
Baier, Carlos J. 
Evans, Luke S. 
Williamson, Philip, T. F. 
Fantini, Jacques 
Barrantes, Francisco José 
Palabras clave : COLESTEROLPROTEINASNEUROTRANSMISORES
Fecha de publicación : 2017
Editorial : Elsevier
Cita : Di Scala, C., et al. Relevance of CARC and CRAC cholesterol-recognition motifs in the nicotinic azcetylcholine receptor and other membrane-bound receptors [en línea]. Postprint del artículo publicado en Current Topics in Membranes. 2017, 80. doi:10.1016/bs.ctm.2017.05.001. Disponible en: https://repositorio.uca.edu.ar/handle/123456789/1460
Resumen : Abstract: Cholesterol is a ubiquitous neutral lipid, which finely tunes the activity of a wide range of membrane proteins, including neurotransmitter and hormone receptors and ion channels. Given the scarcity of available X-ray crystallographic structures and the even fewer in which cholesterol sites have been directly visualized, application of in silico computational methods remains a valid alternative for the detection and thermodynamic characterization of cholesterol-specific sites in functionally important membrane proteins. The membrane-embedded segments of the paradigm neurotransmitter receptor for acetylcholine display a series of cholesterol consensus domains (which we have coined “CARC”). The CARC motif exhibits a preference for the outer membrane leaflet and its mirror motif, CRAC, for the inner one. Some membrane proteins possess the double CARC–CRAC sequences within the same transmembrane domain. In addition to in silico molecular modeling, the affinity, concentration dependence, and specificity of the cholesterol-recognition motif–protein interaction have recently found experimental validation in other biophysical approaches like monolayer techniques and nuclear magnetic resonance spectroscopy. From the combined studies, it becomes apparent that the CARC motif is now more firmly established as a high-affinity cholesterol-binding domain for membrane-bound receptors and remarkably conserved along phylogenetic evolution.
URI : https://repositorio.uca.edu.ar/handle/123456789/1460
ISSN : 1063-5823
Disciplina: MEDICINA
DOI: 10.1016/bs.ctm.2017.05.001
Derechos: Acceso Abierto. 1 año de embargo
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