{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,6]],"date-time":"2026-05-06T02:22:57Z","timestamp":1778034177533,"version":"3.51.4"},"reference-count":88,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2020,7,27]],"date-time":"2020-07-27T00:00:00Z","timestamp":1595808000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100011011","name":"Junta de Andaluc\u00eda","doi-asserted-by":"publisher","award":["CVI-5915"],"award-info":[{"award-number":["CVI-5915"]}],"id":[{"id":"10.13039\/501100011011","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Life"],"abstract":"<jats:p>The PDZ domain (PSD95-Discs large-ZO1) is a widespread modular domain present in the living organisms. A prevalent function in the PDZ family is to serve as scaffolding 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\u2013activity 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.<\/jats:p>","DOI":"10.3390\/life10080123","type":"journal-article","created":{"date-parts":[[2020,7,27]],"date-time":"2020-07-27T09:24:49Z","timestamp":1595841889000},"page":"123","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["The Conformational Plasticity Vista of PDZ Domains"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8667-1651","authenticated-orcid":false,"given":"Javier","family":"Murciano-Calles","sequence":"first","affiliation":[{"name":"Departamento de Qu\u00edmica F\u00edsica, Unidad de Excelencia de Qu\u00edmica Aplicada a Biomedicina y Medioambiente, Facultad de Ciencias, Universidad de Granada, 18071 Granada, Spain"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2020,7,27]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"6323","DOI":"10.1039\/C3CP54226B","article-title":"The binding mechanisms of intrinsically disordered proteins","volume":"16","author":"Dogan","year":"2014","journal-title":"Phys. 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