The Conformational Plasticity Vista of PDZ Domains Murciano Calles, Javier PDZ domains PSD95 Protein folding Ligand binding Allostery Post-translational modification Part of this researchwas funded by the Andalusian Regional Government (http://www.juntadeandalucia.es) [grant number CVI-5915], and the author currently acknowledges funds from a reincorporation contract from the University of Granada. 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. 2020-11-09T10:01:56Z 2020-11-09T10:01:56Z 2020-07-27 journal article Murciano-Calles, J. The Conformational Plasticity Vista of PDZ Domains. Life 2020, 10, 123. [doi:10.3390/life10080123] http://hdl.handle.net/10481/64137 10.3390/life10080123 eng http://creativecommons.org/licenses/by/3.0/es/ open access Atribución 3.0 España MDPI