@misc{10481/96051,
year = {2016},
month = {1},
url = {https://hdl.handle.net/10481/96051},
abstract = {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. Results showed that all domains passed through a common intermediate,
which populated upon unfolding, and that this in turn drove the misfolding towards worm-like fibrillar
structures. Thus, the unfolding/misfolding behaviour appears to be shared within these domains. We
have also analyzed how this landscape can be modified upon the inclusion of extra-elements, as it is in
the nNOS PDZ domain, or the organization of swapped species, as happens in the second PDZ domain
of the ZO2 protein. Although the intermediates still formed upon thermal unfolding, the misfolding was
prevented to varying degrees.},
organization = {Grants CVI-5915 from the Junta de Andalucía},
organization = {BIO2012-39922-C02 from the
Ministerio de Economia y Competitividad and FEDER},
organization = {PI13-01330 from Instituto de Salud Carlos III and
SGR09-0761 from the Generalitat de Catalunya},
organization = {Ministerio de
Economia y Competitividad and presently acknowledges financial support from the Alfonso Martín Escudero
Foundation},
publisher = {Springer Nature},
title = {Common features in the unfolding and misfolding of PDZ domains and beyond: the modulatory effect of domain swapping and extraelements},
doi = {10.1038/srep19242},
author = {Murciano Calles, Javier and Güell-Bosch, Jofre and Villegas, Sandra and Martinez, Jose C.},
}