{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gregory E"],"funding":["NCI NIH HHS","Florida Department of Health Project","NIH","NIGMS NIH HHS"],"pagination":["1558"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9687289"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(11)"],"pubmed_abstract":["An intramolecular interaction between the p53 transactivation and DNA binding domains inhibits DNA binding. To study this autoinhibition, we used a fragment of p53, referred to as ND WT, containing the N-terminal transactivation domains (TAD1 and TAD2), a proline rich region (PRR), and the DNA binding domain (DBD). We mutated acidic, nonpolar, and aromatic amino acids in TAD2 to disrupt the interaction with DBD and measured the effects on DNA binding affinity at different ionic strengths using fluorescence anisotropy. We observed a large increase in DNA binding affinity for the mutants consistent with reduced autoinhibition. The ΔΔG between DBD and ND WT for binding a consensus DNA sequence is -3.0 kcal/mol at physiological ionic strength. ΔΔG increased to -1.03 kcal/mol when acidic residu"],"journal":["Biomolecules"],"pubmed_title":["Sequence Properties of An Intramolecular Interaction That Inhibits p53 DNA Binding."],"pmcid":["PMC9687289"],"funding_grant_id":["R01CA141244","R01GM115556","R01 CA141244","R01 GM115556","20B17"],"pubmed_authors":["Gregory E","Daughdrill GW"],"additional_accession":[]},"is_claimable":false,"name":"Sequence Properties of An Intramolecular Interaction That Inhibits p53 DNA Binding.","description":"An intramolecular interaction between the p53 transactivation and DNA binding domains inhibits DNA binding. To study this autoinhibition, we used a fragment of p53, referred to as ND WT, containing the N-terminal transactivation domains (TAD1 and TAD2), a proline rich region (PRR), and the DNA binding domain (DBD). We mutated acidic, nonpolar, and aromatic amino acids in TAD2 to disrupt the interaction with DBD and measured the effects on DNA binding affinity at different ionic strengths using fluorescence anisotropy. We observed a large increase in DNA binding affinity for the mutants consistent with reduced autoinhibition. The ΔΔG between DBD and ND WT for binding a consensus DNA sequence is -3.0 kcal/mol at physiological ionic strength. ΔΔG increased to -1.03 kcal/mol when acidic residu","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2026-05-08T03:11:06.041Z","creation":"2025-04-21T14:12:37.14Z"},"accession":"S-EPMC9687289","cross_references":{"pubmed":["36358908"],"doi":["10.3390/biom12111558"]}}