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TitleCryo-EM structure of human HCN3 channel and its regulation by cAMP.
Journal, issue, pagesJ Biol Chem, Vol. 300, Issue 6, Page 107288, Year 2024
Publish dateApr 16, 2024
AuthorsBo Yu / Qiuyuan Lu / Jian Li / Xinyu Cheng / Han Hu / Yuanshuo Li / Tong Che / Yaoguang Hua / Haihai Jiang / Yuting Zhang / Cuiling Xian / Tingting Yang / Ying Fu / Yixiang Chen / Weiwei Nan / Peter J McCormick / Bing Xiong / Jingjing Duan / Bo Zeng / Yanyan Li / Yang Fu / Jin Zhang /
PubMed AbstractHCN channels are important for regulating heart rhythm and nerve activity and have been studied as potential drug targets for treating depression, arrhythmia, nerve pain, and epilepsy. Despite ...HCN channels are important for regulating heart rhythm and nerve activity and have been studied as potential drug targets for treating depression, arrhythmia, nerve pain, and epilepsy. Despite possessing unique pharmacological properties, HCN channels share common characteristics in that they are activated by hyperpolarization and modulated by cAMP and other membrane lipids. However, the mechanisms of how these ligands bind and modulate HCN channels are unclear. In this study, we solved structures of full-length human HCN3 using cryo-EM and captured two different states, including a state without any ligand bound and a state with cAMP bound. Our structures reveal the novel binding sites for cholesteryl hemisuccinate in apo state and show how cholesteryl hemisuccinate and cAMP binding cause conformational changes in different states. These findings explain how these small modulators are sensed in mammals at the molecular level. The results of our study could help to design more potent and specific compounds to influence HCN channel activity and offer new therapeutic possibilities for diseases that lack effective treatment.
External linksJ Biol Chem / PubMed:38636662 / PubMed Central
MethodsEM (single particle)
Resolution2.72 Å
Structure data

35602

8inz

EMDB-35602, PDB-8inz:
Cryo-EM structure of human HCN3 channel in apo state
Method: EM (single particle) / Resolution: 2.72 Å

Chemicals


ChemComp, No image

ChemComp-VX9:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / human HCN3 channel

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