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http://purl.uniprot.org/citations/37683642http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37683642http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37683642http://www.w3.org/2000/01/rdf-schema#comment"Interferon regulatory factor 4 (IRF4) is a transcription factor that regulates the development and function of immune cells. Recently, a new multimorphic mutation T95R was identified in the IRF4 DNA-binding domain (DBD) in patients with autosomal dominant combined immune deficiency. Here, we characterized the interactions of the wild-type IRF4-DBD (IRF4-DBDWT) and T95R mutant (IRF4-DBDT95R) with a canonical DNA sequence and several noncanonical DNA sequences. We found that compared to IRF4-DBDWT, IRF4-DBDT95R exhibits higher binding affinities for both canonical and noncanonical DNAs, with the highest preference for the noncanonical GATA sequence. The crystal structures of IRF4-DBDWT in complex with the GATA sequence and IRF4-DBDT95R in complexes with both canonical and noncanonical DNAs were determined, showing that the T95R mutation enhances the interactions of IRF4-DBDT95R with the canonical and noncanonical DNAs to achieve higher affinity and specificity. Collectively, our data provide the molecular basis for the gain-of-function and new function of IRF4T95R."xsd:string
http://purl.uniprot.org/citations/37683642http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2023.08.013"xsd:string
http://purl.uniprot.org/citations/37683642http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2023.08.013"xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/author"Ding J."xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/author"Ding J."xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/author"Feng X."xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/author"Feng X."xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/author"Wang G."xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/author"Wang G."xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/pages"1441-1451.e3"xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/pages"1441-1451.e3"xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/title"Molecular basis for the functional roles of the multimorphic T95R mutation of IRF4 causing human autosomal dominant combined immunodeficiency."xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/title"Molecular basis for the functional roles of the multimorphic T95R mutation of IRF4 causing human autosomal dominant combined immunodeficiency."xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/volume"31"xsd:string
http://purl.uniprot.org/citations/37683642http://purl.uniprot.org/core/volume"31"xsd:string
http://purl.uniprot.org/citations/37683642http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37683642
http://purl.uniprot.org/citations/37683642http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37683642
http://purl.uniprot.org/citations/37683642http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/37683642
http://purl.uniprot.org/citations/37683642http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/37683642