How cholesterol interacts with membrane proteins : an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains

Abstract: The plasma membrane of eukaryotic cells contains several types of lipids displaying high biochemical variability in both their apolar moiety (e.g., the acyl chain of glycerolipids) and their polar head (e.g., the sugar structure of glycosphingolipids). Among these lipids, cholesterol is un...

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Detalles Bibliográficos
Autores principales: Fantini, Jacques, Barrantes, Francisco José
Formato: Artículo
Lenguaje:Inglés
Publicado: Frontiers 2019
Materias:
NEUROTRANSMISORES
COLESTEROL
PROTEINAS
ENFERMEDAD DE ALZHEIMER
RECEPTORES
Acceso en línea:https://repositorio.uca.edu.ar/handle/123456789/8763
Aporte de:
Repositorio Institucional de la Universidad Católica Argentina (UCA) de Universidad Católica Argentina
id I33-R139123456789-8763
record_format dspace
institution Universidad Católica Argentina
institution_str I-33
repository_str R-139
collection Repositorio Institucional de la Universidad Católica Argentina (UCA)
language Inglés
topic NEUROTRANSMISORES
COLESTEROL
PROTEINAS
ENFERMEDAD DE ALZHEIMER
RECEPTORES
spellingShingle NEUROTRANSMISORES
COLESTEROL
PROTEINAS
ENFERMEDAD DE ALZHEIMER
RECEPTORES
Fantini, Jacques
Barrantes, Francisco José
How cholesterol interacts with membrane proteins : an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
topic_facet NEUROTRANSMISORES
COLESTEROL
PROTEINAS
ENFERMEDAD DE ALZHEIMER
RECEPTORES
description Abstract: The plasma membrane of eukaryotic cells contains several types of lipids displaying high biochemical variability in both their apolar moiety (e.g., the acyl chain of glycerolipids) and their polar head (e.g., the sugar structure of glycosphingolipids). Among these lipids, cholesterol is unique because its biochemical variability is almost exclusively restricted to the oxidation of its polar -OH group. Although generally considered the most rigid membrane lipid, cholesterol can adopt a broad range of conformations due to the flexibility of its isooctyl chain linked to the polycyclic sterane backbone. Moreover, cholesterol is an asymmetric molecule displaying a planar α face and a rough β face. Overall, these structural features open up a number of possible interactions between cholesterol and membrane lipids and proteins, consistent with the prominent regulatory functions that this unique lipid exerts on membrane components. The aim of this review is to describe how cholesterol interacts with membrane lipids and proteins at the molecular/atomic scale, with special emphasis on transmembrane domains of proteins containing either the consensus cholesterol-binding motifs CRAC and CARC or a tilted peptide. Despite their broad structural diversity, all these domains bind cholesterol through common molecular mechanisms, leading to the identification of a subset of amino acid residues that are overrepresented in both linear and three-dimensional membrane cholesterol-binding sites.
format Artículo
author Fantini, Jacques
Barrantes, Francisco José
author_facet Fantini, Jacques
Barrantes, Francisco José
author_sort Fantini, Jacques
title How cholesterol interacts with membrane proteins : an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
title_short How cholesterol interacts with membrane proteins : an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
title_full How cholesterol interacts with membrane proteins : an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
title_fullStr How cholesterol interacts with membrane proteins : an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
title_full_unstemmed How cholesterol interacts with membrane proteins : an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains
title_sort how cholesterol interacts with membrane proteins : an exploration of cholesterol-binding sites including crac, carc, and tilted domains
publisher Frontiers
publishDate 2019
url https://repositorio.uca.edu.ar/handle/123456789/8763
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