{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Haußermann K"],"funding":["European Research Council","Deutsche Forschungsgemeinschaft"],"pagination":["7662-7667"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6986896"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["58(23)"],"pubmed_abstract":["Protein-protein and protein-substrate interactions are critical to function and often depend on factors that are difficult to disentangle. Herein, a combined biochemical and biophysical approach, based on electrically switchable DNA biochips and single-molecule mass analysis, was used to characterize the DNA binding and protein oligomerization of the transcription factor, forkhead box protein P2 (FOXP2). FOXP2 contains domains commonly involved in nucleic-acid binding and protein oligomerization, such as a C<sub>2</sub> H<sub>2</sub> -zinc finger (ZF), and a leucine zipper (LZ), whose roles in FOXP2 remain largely unknown. We found that the LZ mediates FOXP2 dimerization via coiled-coil formation but also contributes to DNA binding. The ZF contributes to protein dimerization when the LZ co"],"journal":["Angewandte Chemie (International ed. in English)"],"pubmed_title":["Dissecting FOXP2 Oligomerization and DNA Binding."],"pmcid":["PMC6986896"],"funding_grant_id":["Leibniz Program","724261","SFB863 TP A9","Starting Grant #337757 (to PK)","Consolidator Grant #724261 (to HD)","337757","256270"],"pubmed_authors":["Dietz H","Young G","Haußermann K","Kukura P"],"additional_accession":[]},"is_claimable":false,"name":"Dissecting FOXP2 Oligomerization and DNA Binding.","description":"Protein-protein and protein-substrate interactions are critical to function and often depend on factors that are difficult to disentangle. Herein, a combined biochemical and biophysical approach, based on electrically switchable DNA biochips and single-molecule mass analysis, was used to characterize the DNA binding and protein oligomerization of the transcription factor, forkhead box protein P2 (FOXP2). FOXP2 contains domains commonly involved in nucleic-acid binding and protein oligomerization, such as a C<sub>2</sub> H<sub>2</sub> -zinc finger (ZF), and a leucine zipper (LZ), whose roles in FOXP2 remain largely unknown. We found that the LZ mediates FOXP2 dimerization via coiled-coil formation but also contributes to DNA binding. The ZF contributes to protein dimerization when the LZ co","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Jun","modification":"2026-05-06T21:25:49.874Z","creation":"2020-05-22T10:49:13Z"},"accession":"S-EPMC6986896","cross_references":{"pubmed":["30887622"],"doi":["10.1002/anie.201901734"]}}