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dc.contributor.author
Favretto, F.
dc.contributor.author
Assfalg, M.
dc.contributor.author
Gallo, Mariana
dc.contributor.author
Cicero, D. O.
dc.contributor.author
D' Onofrio, M. D.
dc.contributor.author
Molinari, H.
dc.date.available
2017-07-03T14:37:21Z
dc.date.issued
2013-09
dc.identifier.citation
Favretto, F.; Assfalg, M.; Gallo, Mariana; Cicero, D. O.; D' Onofrio, M. D.; et al.; Ligand binding promiscuity of human liver fatty acid binding protein: structural and dynamic insights from an interaction study with glycocholate and oleate; Wiley Vch Verlag; Chembiochem; 14; 9-2013; 1087-1819
dc.identifier.issn
1439-4227
dc.identifier.uri
http://hdl.handle.net/11336/19373
dc.description.abstract
Human liver fatty acid binding protein (hL-FABP) has been reported to act as an intracellular shuttle of lipid molecules, playing a central role in systemic metabolic homeostasis. The involvement of hL-FABP in the transport of bile salts has been postulated but scarcely investigated. Here we describe a thorough NMR investigation of glycocholate (GCA) binding to hL-FABP. The protein proved able to bind a single molecule of GCA in contrast with the 1:2 stoichiometry observed with fatty acids. GCA was found to occupy the large internal cavity of hL-FABP without requiring major conformational rearrangements of the protein backbone but leading to an increased stability, similar to that estimated for the hL-FABP:oleate complex. Fast time scale dynamics appeared not significantly perturbed in the presence of ligands. Slow motions, at variance with other proteins of the family, were retained or enhanced upon binding and consistent with a requirement of structural plasticity for promiscuous recognition.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Vch Verlag
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Protein
dc.subject
Structure
dc.subject
Dynamics
dc.subject.classification
Biofísica
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Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Ligand binding promiscuity of human liver fatty acid binding protein: structural and dynamic insights from an interaction study with glycocholate and oleate
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-09-05T13:12:46Z
dc.journal.volume
14
dc.journal.pagination
1087-1819
dc.journal.pais
Alemania
dc.journal.ciudad
Weinheim
dc.description.fil
Fil: Favretto, F.. Universita Di Verona; Italia
dc.description.fil
Fil: Assfalg, M.. Universita Di Verona; Italia
dc.description.fil
Fil: Gallo, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
dc.description.fil
Fil: Cicero, D. O.. Fundación Instituto Leloir; Argentina. Universita Di Roma; Italia
dc.description.fil
Fil: D' Onofrio, M. D.. Universita Di Verona; Italia
dc.description.fil
Fil: Molinari, H.. Laboratorio NMR, ISMAC-CNR ; Italia
dc.journal.title
Chembiochem
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/10.1002/cbic.201300156


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