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dc.contributor.author
Fantini, J.  
dc.contributor.author
Barrantes, Francisco Jose  
dc.date.available
2016-01-18T19:23:58Z  
dc.date.issued
2013-02-28  
dc.identifier.citation
Fantini, J.; Barrantes, Francisco Jose; How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains; Frontiers; Frontiers in Physiology; 4; 31; 28-2-2013; 1-9  
dc.identifier.issn
1664-042X  
dc.identifier.uri
http://hdl.handle.net/11336/3682  
dc.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.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Frontiers  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/  
dc.subject
Cholesterol  
dc.subject
Membrane  
dc.subject
Protein  
dc.subject
Lipid-Protein Interaction  
dc.subject.classification
Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
How cholesterol interacts with membrane proteins: an exploration of cholesterol-binding sites including CRAC, CARC, and tilted domains  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2016-03-30 10:35:44.97925-03  
dc.journal.volume
4  
dc.journal.number
31  
dc.journal.pagination
1-9  
dc.journal.pais
Suiza  
dc.journal.ciudad
Lausanne  
dc.conicet.avisoEditorial
This Document is Protected by copyright and was first published by Frontiers. All rights reserved. it is reproduced with permission  
dc.description.fil
Fil: Fantini, J.. Aix-Marseille Université. Interactions Moléculaires et Systèmes Membranaires; Francia  
dc.description.fil
Fil: Barrantes, Francisco Jose. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Facultad de Ciencias Médicas. Instituto de Investigaciones Biomédicas; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina  
dc.journal.title
Frontiers in Physiology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://journal.frontiersin.org/article/10.3389/fphys.2013.00031/abstract  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3389/fphys.2013.00031  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/issn/1664-042X  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3584320/