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Study of the molecular recognition of novel fungal transglycosylase ligands

AutorDelso, J. Ignacio; Gomollón-Bel, Fernando ; Valero-González, Jessika; Marca, Eduardo ; Tejero, Tomás ; Hurtado-Guerrero, Ramón; Merino, Pedro
Fecha de publicación2016
CitaciónBIFI 2016
ResumenFungi cell wall remodeling is controlled by the equilibrium between glycoside hydrolases, glycosyltransferases, and transglycosylases. Family 72 glycoside hydrolases (GH72) are ubiquitous in fungal organisms and are known to possess significant transglycosylase activity, producing elongated beta(1-3) glucan chains. Among them are the Gas (in S. cerevisiae), Gel (in A. fumigates) or Phr and Pga (in C. albicans), and all of them with a well conserved catalytic site. The only protein whose structure has been resolved within this family is ScGas2, which will be our model for ligands and inhibitors design. In this communication, they will be presented the design, synthesis and the study of the molecular recognition of novel beta(1-3)glucan-based ligands with ScGas2. To characterize the protein-ligand interactions several techniques were employed, such as saturation transfer difference NMR experiments (STD-NMR), molecular docking, molecular dynamics, non-covalent-interaction calculation (NCI) and X-ray diffraction of protein complexes.
DescripciónResumen del trabajo presentado a la VII International Conference on Molecular Recognition, celebrada en Zaragoza (España) del 1 al 3 de febrero de 2016.
URIhttp://hdl.handle.net/10261/156174
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