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

Fernandez Pacios, Luis; Gomez Casado, Cristina; Tordesillas Villuendas, Leticia; Palacín Gómez, Aranzazu; Sanchez-Monge Laguna De Rins, Maria Rosa y 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.

Descripción

Título: Computational study of ligand binding in lipid transfer proteins: Structures, interfaces, and free energies of protein-lipid complexes
Autor/es:
  • Fernandez Pacios, Luis
  • Gomez Casado, Cristina
  • Tordesillas Villuendas, Leticia
  • Palacín Gómez, Aranzazu
  • Sanchez-Monge Laguna De Rins, Maria Rosa
  • Díaz Perales, Araceli
Tipo de Documento: Artículo
Título de Revista/Publicación: Journal of Computational Chemistry
Fecha: 2012
Volumen: 33
Materias:
Escuela: E.T.S.I. Montes (UPM) [antigua denominación]
Departamento: Biotecnologia [hasta 2014]
Licencias Creative Commons: Reconocimiento - Sin obra derivada - No comercial

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Resumen

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.

Más información

ID de Registro: 15467
Identificador DC: http://oa.upm.es/15467/
Identificador OAI: oai:oa.upm.es:15467
Depositado por: Memoria Investigacion
Depositado el: 25 Mar 2014 12:56
Ultima Modificación: 04 Mar 2015 16:24
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