{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Moffett AS"],"funding":["state of Illinois","National Science Foundation"],"pagination":["2354-2363"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5768518"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["113(11)"],"pubmed_abstract":["Growing evidence supports the importance of protein S-glutathionylation as a regulatory post-translational modification with functional consequences for proteins. Discoveries of redox-state-dependent protein kinase S-glutathionylation have fueled discussion of redox-sensitive signaling. Following previously published experimental evidence for S-glutathionylation induced deactivation of the Arabidopsis thaliana kinase BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED RECEPTOR-LIKE KINASE 1 (BAK1), we investigated the consequences of S-glutathionylation on the equilibrium conformational ensemble of BAK1 using all-atom molecular dynamics simulations. We found that glutathionylation of C408 allosterically destabilizes the active-like state of BAK1 and stabilizes an inactive conformation known to recur "],"journal":["Biophysical journal"],"pubmed_title":["Allosteric Control of a Plant Receptor Kinase through S-Glutathionylation."],"pmcid":["PMC5768518"],"funding_grant_id":["OCI-0725070","ACI-1238993"],"pubmed_authors":["Huber SC","Shukla D","Bender KW","Moffett AS"],"additional_accession":[]},"is_claimable":false,"name":"Allosteric Control of a Plant Receptor Kinase through S-Glutathionylation.","description":"Growing evidence supports the importance of protein S-glutathionylation as a regulatory post-translational modification with functional consequences for proteins. Discoveries of redox-state-dependent protein kinase S-glutathionylation have fueled discussion of redox-sensitive signaling. Following previously published experimental evidence for S-glutathionylation induced deactivation of the Arabidopsis thaliana kinase BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED RECEPTOR-LIKE KINASE 1 (BAK1), we investigated the consequences of S-glutathionylation on the equilibrium conformational ensemble of BAK1 using all-atom molecular dynamics simulations. We found that glutathionylation of C408 allosterically destabilizes the active-like state of BAK1 and stabilizes an inactive conformation known to recur ","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Dec","modification":"2026-04-15T19:27:34.471Z","creation":"2026-04-07T14:01:33.824Z"},"accession":"S-EPMC5768518","cross_references":{"pubmed":["29211989"],"doi":["10.1016/j.bpj.2017.08.059"]}}