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TitleStructure basis for the activation of KCNQ2 by endogenous and exogenous ligands.
Journal, issue, pagesCell Rep, Vol. 45, Issue 1, Page 116771, Year 2025
Publish dateDec 23, 2025
AuthorsYiwen Zhao / Zhenni Yang / Sai Shi / Han Hao / Xinmeng Li / Demin Ma / Nannan Su / Weixin Zhao / Jicheng Shao / Yating An / Ke Wang / Yinuo Liu / Lu Zou / Jinlong Qi / Hailin Zhang / Jiangtao Guo / Xiaona Du /
PubMed AbstractThe voltage-gated potassium channel KCNQ2 is crucial for stabilizing neuronal membrane potential, and its mutations can cause various epilepsies. KCNQ2 is activated by endogenous ligand ...The voltage-gated potassium channel KCNQ2 is crucial for stabilizing neuronal membrane potential, and its mutations can cause various epilepsies. KCNQ2 is activated by endogenous ligand phosphatidylinositol-4,5-bisphosphate (PIP) and exogenous ligands, yet the structural mechanisms underlying these activations remain unclear. Here, we report the cryo-electron microscopy structures of human KCNQ2 in complex with exogenous ligands QO-58 and QO-83 in the absence or presence of PIP in either closed or open conformation. While QO-83 binds in the classical fenestration pocket of the pore domain, QO-58 mainly binds at the flank of S4 in the voltage-sensing domain. These structures, along with electrophysiological assays and computational studies, provide mechanistic insights into the ligand activation of KCNQ2 and may guide the development of anti-epileptic drugs targeting KCNQ2.
External linksCell Rep / PubMed:41442279
MethodsEM (single particle)
Resolution2.9 - 3.8 Å
Structure data

38522

8xo1

EMDB-38522, PDB-8xo1:
Human KCNQ2-CaM in complex with QO-83
Method: EM (single particle) / Resolution: 3.8 Å

62892

9l8w

EMDB-62892, PDB-9l8w:
Human KCNQ2-CaM in complex with QO-58
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

PDB-1lwz:
Unknown entry

PDB-1lvr:
IC3 of CB1 (L431A,A432L) Bound to G(alpha)i

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / KCNQ2 / human voltage-gated potassium channel

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