Modeling iron-catecholates binding to NGAL protein

Gomez Casado, Cristina and Roth Walter, Franziska and Jensen Jarolim, Erika and Díaz Perales, Araceli and Fernandez Pacios, Luis (2013). Modeling iron-catecholates binding to NGAL protein. "Journal of Molecular Graphics and Modelling", v. 45 ; pp. 111-121. ISSN 1093-3263.


Title: Modeling iron-catecholates binding to NGAL protein
  • Gomez Casado, Cristina
  • Roth Walter, Franziska
  • Jensen Jarolim, Erika
  • Díaz Perales, Araceli
  • Fernandez Pacios, Luis
Item Type: Article
Título de Revista/Publicación: Journal of Molecular Graphics and Modelling
Date: September 2013
Volume: 45
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Neutrophil gelatinase associated lipocalin (NGAL) protein is attracting a great interest because of its antibacterial properties played upon modulating iron content in competition against iron acquisition processes developed by pathogenic bacteria that bind selective ferric iron chelators (siderophores). Besides its known high affinity to enterobactin, the most important siderophore, it has been recently shown that NGAL is able to bind Fe(III) coordinated by catechols. The selective binding of Fe(III)-catechol ligands to NGAL is here studied by using iron coordination structures with one, two, and three catecholate ligands. By means of a computational approach that consists of B3LYP/6-311G(d,p) quantum calculations for geometries, electron properties and electrostatic potentials of ligands, protein–ligand flexible docking calculations, analyses of protein–ligand interfaces, and Poisson–Boltzmann electrostatic potentials for proteins, we study the binding of iron catecholate ligands to NGAL as a central member of the lipocalin family of proteins. This approach provides a modeling basis for exploring in silico the selective binding of iron catecholates ligands giving a detailed picture of their interactions in terms of electrostatic effects and a network of hydrogen bonds in the protein binding pocket.

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Item ID: 26571
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Deposited by: Memoria Investigacion
Deposited on: 24 Jun 2014 13:13
Last Modified: 30 Sep 2015 22:56
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