{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sun X"],"funding":["Taishan Scholar Project of Shandong Province","National Natural Science Foundation of China","Shandong University","Wellcome Trust","山东省科学技术厅 | Natural Science Fund for Distinguished Young Scholars of Shandong Province","Natural Science Foundation of Jiangsu Province"],"pagination":["e2208804119"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9674253"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["119(46)"],"pubmed_abstract":["Neuronal PER-ARNT-SIM (PAS) domain protein 4 (NPAS4) is a protective transcriptional regulator whose dysfunction has been linked to a variety of neuropsychiatric and metabolic diseases. As a member of the basic helix-loop-helix PER-ARNT-SIM (bHLH-PAS) transcription factor family, NPAS4 is distinguished by an ability to form functional heterodimers with aryl hydrocarbon receptor nuclear translocator (ARNT) and ARNT2, both of which are also bHLH-PAS family members. Here, we describe the quaternary architectures of NPAS4-ARNT and NPAS4-ARNT2 heterodimers in complexes involving DNA response elements. Our crystallographic studies reveal a uniquely interconnected domain conformation for the NPAS4 protein itself, as well as its differentially configured heterodimeric arrangements with both ARNT a"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Structures of NPAS4-ARNT and NPAS4-ARNT2 heterodimers reveal new dimerization modalities in the bHLH-PAS transcription factor family."],"pmcid":["PMC9674253"],"funding_grant_id":["tsqn201909004","ZR2021JQ30","2020QNQT009","210664/Z/18/Z","BK20170399","22177063"],"pubmed_authors":["Jing L","Diao X","Li F","Rastinejad F","Zhang M","Wu D","Sun X","Zhuang J"],"additional_accession":[]},"is_claimable":false,"name":"Structures of NPAS4-ARNT and NPAS4-ARNT2 heterodimers reveal new dimerization modalities in the bHLH-PAS transcription factor family.","description":"Neuronal PER-ARNT-SIM (PAS) domain protein 4 (NPAS4) is a protective transcriptional regulator whose dysfunction has been linked to a variety of neuropsychiatric and metabolic diseases. As a member of the basic helix-loop-helix PER-ARNT-SIM (bHLH-PAS) transcription factor family, NPAS4 is distinguished by an ability to form functional heterodimers with aryl hydrocarbon receptor nuclear translocator (ARNT) and ARNT2, both of which are also bHLH-PAS family members. Here, we describe the quaternary architectures of NPAS4-ARNT and NPAS4-ARNT2 heterodimers in complexes involving DNA response elements. Our crystallographic studies reveal a uniquely interconnected domain conformation for the NPAS4 protein itself, as well as its differentially configured heterodimeric arrangements with both ARNT a","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-05-10T06:50:57.388Z","creation":"2025-02-19T03:25:51.83Z"},"accession":"S-EPMC9674253","cross_references":{"pubmed":["36343253"],"doi":["10.1073/pnas.2208804119"]}}