6Y7Q
Crystal Structure of the N-terminal PAS domain from the hERG3 Potassium Channel
This is a non-PDB format compatible entry.
Summary for 6Y7Q
| Entry DOI | 10.2210/pdb6y7q/pdb |
| Related | 5VA1 5VA2 5VA3 |
| Descriptor | Potassium voltage-gated channel subfamily H member 7, GLYCEROL, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | pas, potassium channel, heme binding, rossmann fold, membrane protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 15608.96 |
| Authors | Cresser-Brown, J.,Raven, E.,Moody, P. (deposition date: 2020-03-02, release date: 2020-08-12, Last modification date: 2024-10-23) |
| Primary citation | Burton, M.J.,Cresser-Brown, J.,Thomas, M.,Portolano, N.,Basran, J.,Freeman, S.L.,Kwon, H.,Bottrill, A.R.,Llansola-Portoles, M.J.,Pascal, A.A.,Jukes-Jones, R.,Chernova, T.,Schmid, R.,Davies, N.W.,Storey, N.M.,Dorlet, P.,Moody, P.C.E.,Mitcheson, J.S.,Raven, E.L. Discovery of a heme-binding domain in a neuronal voltage-gated potassium channel. J.Biol.Chem., 295:13277-13286, 2020 Cited by PubMed Abstract: The EAG () family of voltage-gated K channels are important regulators of neuronal and cardiac action potential firing (excitability) and have major roles in human diseases such as epilepsy, schizophrenia, cancer, and sudden cardiac death. A defining feature of EAG (Kv10-12) channels is a highly conserved domain on the N terminus, known as the eag domain, consisting of a Per-ARNT-Sim (PAS) domain capped by a short sequence containing an amphipathic helix (Cap domain). The PAS and Cap domains are both vital for the normal function of EAG channels. Using heme-affinity pulldown assays and proteomics of lysates from primary cortical neurons, we identified that an EAG channel, hERG3 (Kv11.3), binds to heme. In whole-cell electrophysiology experiments, we identified that heme inhibits hERG3 channel activity. In addition, we expressed the Cap and PAS domain of hERG3 in and, using spectroscopy and kinetics, identified the PAS domain as the location for heme binding. The results identify heme as a regulator of hERG3 channel activity. These observations are discussed in the context of the emerging role for heme as a regulator of ion channel activity in cells. PubMed: 32723862DOI: 10.1074/jbc.RA120.014150 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.39 Å) |
Structure validation
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