The Conformational Plasticity Vista of PDZ Domains
Metadatos
Mostrar el registro completo del ítemAutor
Murciano Calles, JavierEditorial
MDPI
Materia
PDZ domains PSD95 Protein folding Ligand binding Allostery Post-translational modification
Fecha
2020-07-27Referencia bibliográfica
Murciano-Calles, J. The Conformational Plasticity Vista of PDZ Domains. Life 2020, 10, 123. [doi:10.3390/life10080123]
Patrocinador
Andalusian Regional Government CVI-5915; University of GranadaResumen
The PDZ domain (PSD95-Discs large-ZO1) is a widespread modular domain present in the
living organisms. Aprevalent function in the PDZ family is to serve as sca olding and adaptor proteins
connecting multiple partners in signaling pathways. An explanation of the flexible functionality in this
domain family, based just on a static perspective of the structure–activity relationship, might fall short.
More dynamic and conformational aspects in the protein fold can be the reasons for such functionality.
Folding studies indeed showed an ample and malleable folding landscape for PDZ domains where
multiple intermediate states were experimentally detected. Allosteric phenomena that resemble
energetic coupling between residues have also been found in PDZ domains. Additionally, several PDZ
domains are modulated by post-translational modifications, which introduce conformational switches
that affect binding. Altogether, the ability to connect diverse partners might arise from the intrinsic
plasticity of the PDZ fold.