{"doi":"10.1073/pnas.2007201117","title":"Supertertiary protein structure affects an allosteric network","abstract":"<jats:title>Significance</jats:title>\n                  <jats:p>Protein function can be allosterically regulated by changes in structure or dynamics. PDZ domains are classic examples for studies of allostery in single protein domains. However, PDZ domains are often found in multidomain proteins; in particular, PDZ3 is located in a supramodule containing three domains. The allosteric network in PDZ3 has never been studied in the presence of the adjacent domains. Here we map the allosteric network for a PDZ3:ligand complex, both in isolation and in the context of a supramodule. We demonstrate that the allosteric network is highly dependent on this supertertiary structure, with broad implications for studies of allostery in single domains.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":2020,"id":25370,"datarank":1.2837796664983299,"base_score":3.58351893845611,"endowment":3.58351893845611,"self_citation_contribution":0.5375278407684165,"citation_network_contribution":0.7462518257299133,"self_endowment_contribution":0.5375278407684165,"citer_contribution":0.7462518257299133,"corpus_percentile":null,"corpus_rank":null,"citation_count":35,"citer_count":23,"citers_with_citation_signal":22,"citers_with_endowment":22,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":149420,"name":"Johanna Kliche","orcid":null,"position":1,"is_corresponding":false},{"id":147237,"name":"Stefano Gianni","orcid":null,"position":2,"is_corresponding":false},{"id":147238,"name":"Per Jemth","orcid":"0000-0003-1516-7228","position":3,"is_corresponding":false},{"id":149419,"name":"Louise Laursen","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":3.58351893845611,"endowment":3.58351893845611,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"32929026","pmcid":"PMC7533695","openalex_id":"https://openalex.org/W3086170770","authors":[],"funders":[{"funder_name":"EC | Horizon 2020","grant_id":"67341","title":null},{"funder_name":"Vetenskapsrådet","grant_id":"2016‐04965","title":null},{"funder_name":"Swedish Research Council","grant_id":"unidentified","title":"unidentified"},{"funder_name":"European Commission","grant_id":"675341","title":"Unraveling Principles of PDZ-mediated Cell Signaling"}],"total_grants":4,"fwci":2.0838,"citation_percentile":0.87831613,"influential_citations":4,"citation_trend":[{"year":2020,"count":1},{"year":2021,"count":9},{"year":2022,"count":8},{"year":2023,"count":7},{"year":2024,"count":5},{"year":2025,"count":3},{"year":2026,"count":2}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"https://www.pnas.org/content/pnas/117/39/24294.full.pdf","host_type":"journal"},{"url":"https://www.pnas.org/content/pnas/117/39/24294.full.pdf","host_type":"HYBRID"},{"url":"https://www.pnas.org/content/pnas/117/39/24294.full.pdf","host_type":"publisher"},{"url":"http://www.pnas.org/syndication/doi/10.1073/pnas.2007201117","host_type":"publisher"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.2007201117","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.2007201117","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/32929026","host_type":"repository"},{"url":"http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-424583","host_type":"repository"},{"url":"http://hdl.handle.net/11573/1464543","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/7533695","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC7533695","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC7533695?pdf=render","host_type":"Europe_PMC"},{"url":"https://doi.org/10.1101/2020.03.24.005553","host_type":""},{"url":"http://dx.doi.org/10.1073/pnas.2007201117","host_type":""},{"url":"https://dx.doi.org/10.1101/2020.03.24.005553","host_type":""},{"url":"https://dx.doi.org/10.1073/pnas.2007201117","host_type":""},{"url":"https://hdl.handle.net/11573/1464543","host_type":""},{"url":"http://dx.doi.org/10.1101/2020.03.24.005553","host_type":""}],"fields_of_study":["Protein Structure and Dynamics","Enzyme Structure and Function","Neurobiology and Insect Physiology Research","Chemistry","Medicine","Biology","0301 basic medicine","0303 health sciences","03 medical and health sciences","Allosteric Regulation","Kinetics","Ligands","Mutation","PDZ Domains","Protein Conformation","Proteins"],"mesh_terms":["Allosteric Regulation","Kinetics","Ligands","Mutation","Protein Conformation","Proteins","PDZ Domains"],"keywords":["PDZ domain","Allosteric regulation","Context (archaeology)","Allosteric enzyme","Ligand (biochemistry)","Protein structure","Chemistry","Biophysics","Crystallography","Computational biology","Biochemistry","Biology","Enzyme","Receptor","Kinetics","protein interactions","Allostery","Double-mutant Cycle","Supertertiary Structure","Molekylärbiologi","Protein Conformation","Biochemistry and Molecular Biology","PDZ Domains","Proteins","Biological Sciences","Ligands","Mutation","protein folding; 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