{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Freeman SL"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["19911-19916"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6778266"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["116(40)"],"pubmed_abstract":["The circadian clock is an endogenous time-keeping system that is ubiquitous in animals and plants as well as some bacteria. In mammals, the clock regulates the sleep-wake cycle via 2 basic helix-loop-helix PER-ARNT-SIM (bHLH-PAS) domain proteins-CLOCK and BMAL1. There is emerging evidence to suggest that heme affects circadian control, through binding of heme to various circadian proteins, but the mechanisms of regulation are largely unknown. In this work we examine the interaction of heme with human CLOCK (hCLOCK). We present a crystal structure for the PAS-A domain of hCLOCK, and we examine heme binding to the PAS-A and PAS-B domains. UV-visible and electron paramagnetic resonance spectroscopies are consistent with a bis-histidine ligated heme species in solution in the oxidized (ferric)"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Heme binding to human CLOCK affects interactions with the E-box."],"pmcid":["PMC6778266"],"funding_grant_id":["BB/L006626/1"],"pubmed_authors":["Fielding AJ","Fairall L","Svistunenko DA","Portolano N","Kyriacou CP","Raven EL","Parkin G","Basran J","Freeman SL","Kwon H","Schwabe JWR","Venkatraman Girija U","Moody PCE"],"additional_accession":[]},"is_claimable":false,"name":"Heme binding to human CLOCK affects interactions with the E-box.","description":"The circadian clock is an endogenous time-keeping system that is ubiquitous in animals and plants as well as some bacteria. In mammals, the clock regulates the sleep-wake cycle via 2 basic helix-loop-helix PER-ARNT-SIM (bHLH-PAS) domain proteins-CLOCK and BMAL1. There is emerging evidence to suggest that heme affects circadian control, through binding of heme to various circadian proteins, but the mechanisms of regulation are largely unknown. In this work we examine the interaction of heme with human CLOCK (hCLOCK). We present a crystal structure for the PAS-A domain of hCLOCK, and we examine heme binding to the PAS-A and PAS-B domains. UV-visible and electron paramagnetic resonance spectroscopies are consistent with a bis-histidine ligated heme species in solution in the oxidized (ferric)","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Oct","modification":"2026-05-01T22:44:21.959Z","creation":"2020-11-08T09:14:32Z"},"accession":"S-EPMC6778266","cross_references":{"pubmed":["31527239"],"doi":["10.1073/pnas.1905216116"]}}