Computational study of ligand binding in lipid transfer proteins: Structures, interfaces, and free energies of protein-lipid complexes

Fernandez Pacios, Luis and Gomez Casado, Cristina and Tordesillas Villuendas, Leticia and Palacín Gómez, Aranzazu and Sanchez-Monge Laguna De Rins, Maria Rosa and Díaz Perales, Araceli (2012). Computational study of ligand binding in lipid transfer proteins: Structures, interfaces, and free energies of protein-lipid complexes. "Journal of Computational Chemistry", v. 33 ; pp. 1831-1844.

Description

Title: Computational study of ligand binding in lipid transfer proteins: Structures, interfaces, and free energies of protein-lipid complexes
Author/s:
  • Fernandez Pacios, Luis
  • Gomez Casado, Cristina
  • Tordesillas Villuendas, Leticia
  • Palacín Gómez, Aranzazu
  • Sanchez-Monge Laguna De Rins, Maria Rosa
  • Díaz Perales, Araceli
Item Type: Article
Título de Revista/Publicación: Journal of Computational Chemistry
Date: 2012
Volume: 33
Subjects:
Faculty: E.T.S.I. Montes (UPM)
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Plant nonspecific lipid transfer proteins (nsLTPs) bind a wide variety of lipids, which allows them to perform disparate functions. Recent reports on their multifunctionality in plant growth processes have posed new questions on the versatile binding abilities of these proteins. The lack of binding specificity has been customarily explained in qualitative terms on the basis of a supposed structural flexibility and nonspecificity of hydrophobic protein-ligand interactions. We present here a computational study of protein-ligand complexes formed between five nsLTPs and seven lipids bound in two different ways in every receptor protein. After optimizing geometries inmolecular dynamics calculations, we computed Poisson- Boltzmann electrostatic potentials, solvation energies, properties of the protein-ligand interfaces, and estimates of binding free energies of the resulting complexes. Our results provide the first quantitative information on the ligand abilities of nsLTPs, shed new light into protein-lipid interactions, and reveal new features which supplement commonly held assumptions on their lack of binding specificity.

More information

Item ID: 15467
DC Identifier: http://oa.upm.es/15467/
OAI Identifier: oai:oa.upm.es:15467
Deposited by: Memoria Investigacion
Deposited on: 25 Mar 2014 12:56
Last Modified: 04 Mar 2015 16:24
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