Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations

Acyl-CoA binding proteins (ACBPs) are highly conserved 10 kDa cytosolic proteins that bind medium- and long-chain acyl-CoA esters. They act as intracellular carriers of acyl-CoA and play a role in acyl-CoA metabolism, gene regulation, acyl-CoA-mediated cell signaling, transport-mediated lipid synthe...

Descripción completa

Detalles Bibliográficos
Autores principales: Vallejo, Diego, Zamarreño, Fernando, Guérin, Diego M.A., Grigera, José Raúl, Costabel, Marcelo D.
Formato: Articulo
Lenguaje:Inglés
Publicado: 2009
Materias:
Ciencias Astronómicas
ACBP
HgACBP
Protein-membrane interaction
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/82670
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-82670
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Astronómicas
ACBP
HgACBP
Protein-membrane interaction
spellingShingle Ciencias Astronómicas
ACBP
HgACBP
Protein-membrane interaction
Vallejo, Diego
Zamarreño, Fernando
Guérin, Diego M.A.
Grigera, José Raúl
Costabel, Marcelo D.
Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
topic_facet Ciencias Astronómicas
ACBP
HgACBP
Protein-membrane interaction
description Acyl-CoA binding proteins (ACBPs) are highly conserved 10 kDa cytosolic proteins that bind medium- and long-chain acyl-CoA esters. They act as intracellular carriers of acyl-CoA and play a role in acyl-CoA metabolism, gene regulation, acyl-CoA-mediated cell signaling, transport-mediated lipid synthesis, membrane trafficking and also, ACBPs were indicated as a possible inhibitor of diazepam binding to the GABA-A receptor. To estimate the importance of the non-specific electrostatic energy in the ACBP-membrane interaction, we computationally modeled the interaction of HgACBP with both anionic and neutral membranes. To compute the Free Electrostatic Energy of Binding (dE), we used the Finite Difference Poisson Boltzmann Equation (FDPB) method as implemented in APBS. In the most energetically favorable orientation, ACBP brings charged residues Lys18 and Lys50 and hydrophobic residues Met46 and Leu47 into membrane surface proximity. This conformation suggests that these four ACBP amino acids are most likely to play a leading role in the ACBP-membrane interaction and ligand intake. Thus, we propose that long range electrostatic forces are the first step in the interaction mechanism between ACBP and membranes.
format Articulo
Articulo
author Vallejo, Diego
Zamarreño, Fernando
Guérin, Diego M.A.
Grigera, José Raúl
Costabel, Marcelo D.
author_facet Vallejo, Diego
Zamarreño, Fernando
Guérin, Diego M.A.
Grigera, José Raúl
Costabel, Marcelo D.
author_sort Vallejo, Diego
title Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
title_short Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
title_full Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
title_fullStr Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
title_full_unstemmed Prediction of the most favorable configuration in the ACBP-membrane interaction based on electrostatic calculations
title_sort prediction of the most favorable configuration in the acbp-membrane interaction based on electrostatic calculations
publishDate 2009
url http://sedici.unlp.edu.ar/handle/10915/82670
work_keys_str_mv AT vallejodiego predictionofthemostfavorableconfigurationintheacbpmembraneinteractionbasedonelectrostaticcalculations
AT zamarrenofernando predictionofthemostfavorableconfigurationintheacbpmembraneinteractionbasedonelectrostaticcalculations
AT guerindiegoma predictionofthemostfavorableconfigurationintheacbpmembraneinteractionbasedonelectrostaticcalculations
AT grigerajoseraul predictionofthemostfavorableconfigurationintheacbpmembraneinteractionbasedonelectrostaticcalculations
AT costabelmarcelod predictionofthemostfavorableconfigurationintheacbpmembraneinteractionbasedonelectrostaticcalculations
bdutipo_str Repositorios
_version_ 1764820488509456384

Ejemplares similares