A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study

Autores
Vallejo, Diego Fernando Gustavo; Grigera, Jose Raul; Costabel, Marcelo Daniel
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Acyl-CoA binding protein (ACBP) plays a key role in lipid metabolism, interacting via a partly unknown mechanism with high affinity with long chain fatty acyl-CoAs (LCFA-CoAs). At present there is no study of the microscopic way ligand binding is accomplished. We analyzed this process by molecular dynamics (MDs) simulations. We proposed a computational model of ligand, able to reproduce some evidence from nuclear magnetic resonance (NMR) data, quantitative time resolved fluorometry and X-ray crystallography. We found that a hydrophobic loop, not in the active site, is important for function. Besides, multiple sequence alignment shows hydrophobicity (and not the residues itselves) conservation.
Fil: Vallejo, Diego Fernando Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Grigera, Jose Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Costabel, Marcelo Daniel. Universidad Nacional del Sur. Departamento de Física; Argentina
Materia
Acyl-coenzyme A binding protein;
Molecular dynamics
Long chain fatty acyl-coenzyme A;
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/241788
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/241788
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics studyVallejo, Diego Fernando GustavoGrigera, Jose RaulCostabel, Marcelo DanielAcyl-coenzyme A binding protein;Molecular dynamicsLong chain fatty acyl-coenzyme A;https://purl.org/becyt/ford/1.7https://purl.org/becyt/ford/1Acyl-CoA binding protein (ACBP) plays a key role in lipid metabolism, interacting via a partly unknown mechanism with high affinity with long chain fatty acyl-CoAs (LCFA-CoAs). At present there is no study of the microscopic way ligand binding is accomplished. We analyzed this process by molecular dynamics (MDs) simulations. We proposed a computational model of ligand, able to reproduce some evidence from nuclear magnetic resonance (NMR) data, quantitative time resolved fluorometry and X-ray crystallography. We found that a hydrophobic loop, not in the active site, is important for function. Besides, multiple sequence alignment shows hydrophobicity (and not the residues itselves) conservation.Fil: Vallejo, Diego Fernando Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; ArgentinaFil: Grigera, Jose Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; ArgentinaFil: Costabel, Marcelo Daniel. Universidad Nacional del Sur. Departamento de Física; ArgentinaElsevier Science2008-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/241788Vallejo, Diego Fernando Gustavo; Grigera, Jose Raul; Costabel, Marcelo Daniel; A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study; Elsevier Science; International Journal of Biological Macromolecules; 42; 3; 12-2008; 271-2770141-8130CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141813007002991info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ijbiomac.2007.12.003info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:47:52Zoai:ri.conicet.gov.ar:11336/241788instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:47:52.415CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study
title A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study
spellingShingle A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study
Vallejo, Diego Fernando Gustavo
Acyl-coenzyme A binding protein;
Molecular dynamics
Long chain fatty acyl-coenzyme A;
title_short A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study
title_full A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study
title_fullStr A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study
title_full_unstemmed A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study
title_sort A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study
dc.creator.none.fl_str_mv Vallejo, Diego Fernando Gustavo
Grigera, Jose Raul
Costabel, Marcelo Daniel
author Vallejo, Diego Fernando Gustavo
author_facet Vallejo, Diego Fernando Gustavo
Grigera, Jose Raul
Costabel, Marcelo Daniel
author_role author
author2 Grigera, Jose Raul
Costabel, Marcelo Daniel
author2_role author
author
dc.subject.none.fl_str_mv Acyl-coenzyme A binding protein;
Molecular dynamics
Long chain fatty acyl-coenzyme A;
topic Acyl-coenzyme A binding protein;
Molecular dynamics
Long chain fatty acyl-coenzyme A;
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.7
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Acyl-CoA binding protein (ACBP) plays a key role in lipid metabolism, interacting via a partly unknown mechanism with high affinity with long chain fatty acyl-CoAs (LCFA-CoAs). At present there is no study of the microscopic way ligand binding is accomplished. We analyzed this process by molecular dynamics (MDs) simulations. We proposed a computational model of ligand, able to reproduce some evidence from nuclear magnetic resonance (NMR) data, quantitative time resolved fluorometry and X-ray crystallography. We found that a hydrophobic loop, not in the active site, is important for function. Besides, multiple sequence alignment shows hydrophobicity (and not the residues itselves) conservation.
Fil: Vallejo, Diego Fernando Gustavo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Grigera, Jose Raul. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina
Fil: Costabel, Marcelo Daniel. Universidad Nacional del Sur. Departamento de Física; Argentina
description Acyl-CoA binding protein (ACBP) plays a key role in lipid metabolism, interacting via a partly unknown mechanism with high affinity with long chain fatty acyl-CoAs (LCFA-CoAs). At present there is no study of the microscopic way ligand binding is accomplished. We analyzed this process by molecular dynamics (MDs) simulations. We proposed a computational model of ligand, able to reproduce some evidence from nuclear magnetic resonance (NMR) data, quantitative time resolved fluorometry and X-ray crystallography. We found that a hydrophobic loop, not in the active site, is important for function. Besides, multiple sequence alignment shows hydrophobicity (and not the residues itselves) conservation.
publishDate 2008
dc.date.none.fl_str_mv 2008-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/241788
Vallejo, Diego Fernando Gustavo; Grigera, Jose Raul; Costabel, Marcelo Daniel; A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study; Elsevier Science; International Journal of Biological Macromolecules; 42; 3; 12-2008; 271-277
0141-8130
CONICET Digital
CONICET
url http://hdl.handle.net/11336/241788
identifier_str_mv Vallejo, Diego Fernando Gustavo; Grigera, Jose Raul; Costabel, Marcelo Daniel; A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: A molecular dynamics study; Elsevier Science; International Journal of Biological Macromolecules; 42; 3; 12-2008; 271-277
0141-8130
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0141813007002991
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ijbiomac.2007.12.003
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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