UAB Digital Repository of Documents 2 records found  Search took 0.00 seconds. 
1.
7 p, 899.7 KB Common features in the unfolding and misfolding of PDZ domains and beyond : the modulatory effect of domain swapping and extra-elements / Murciano Calles, Javier (Universidad de Granada. Departamento de Química Física) ; Güell Bosch, Jofre (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Villegas Hernández, Sandra (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Martínez, José C. (Universidad de Granada. Departamento de Química Física)
PDZ domains are protein-protein interaction modules sharing the same structural arrangement. To discern whether they display common features in their unfolding/misfolding behaviour we have analyzed in this work the unfolding thermodynamics, together with the misfolding kinetics, of the PDZ fold using three archetypical examples: the second and third PDZ domains of the PSD95 protein and the Erbin PDZ domain. [...]
2016 - 10.1038/srep19242
Scientific Reports, Vol. 6 (January 2016) , art. 19242  
2.
13 p, 2.6 MB The Impact of Extra-Domain Structures and PostTranslational Modifications in the Folding/Misfolding Behaviour of the Third PDZ Domain of MAGUK Neuronal Protein PSD-95 / Murciano Calles, Javier (Universidad de Granada. Departamento de Química Física) ; Marin Argany, Marta (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Cobos, Eva S. (Universidad de Granada. Departamento de Química Física) ; Villegas Hernández, Sandra (Universitat Autònoma de Barcelona. Departament de Bioquímica i Biologia Molecular) ; Martínez, José C. (Universidad de Granada. Departamento de Química Física)
The modulation of binding affinities and specificities by post-translational modifications located out from the binding pocket of the third PDZ domain of PSD-95 (PDZ3) has been reported recently. It is achieved through an intra-domain electrostatic network involving some charged residues in the β2–β3 loop (were a succinimide modification occurs), the α3 helix (an extra-structural element that links the PDZ3 domain with the following SH3 domain in PSD-95, and contains the phosphorylation target Tyr397), and the ligand peptide. [...]
2014 - 10.1371/journal.pone.0098124
PLoS one, Vol. 9, Num. 5 (2014) , p. e98124  

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