Journal
JOURNAL OF COMPUTATIONAL CHEMISTRY
Volume 33, Issue 22, Pages 1831-1844Publisher
WILEY
DOI: 10.1002/jcc.23012
Keywords
protein-ligand interactions; lipid binding; protein structure; electrostatic potential; solvation effects
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Funding
- Subdireccion General de Proyectos de Investigacion, Spanish Government Training Grants (MEC-FPU and FPI programs)
- Ministerio de Ciencia e Innovacion [BIO2009-07050]
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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 in molecular 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. (c) 2012 Wiley Periodicals, Inc.
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