9l8w

Human KCNQ2-CaM in complex with QO-58

spinqualitylabelsall models 9l8w, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9l8w is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.9Å Ligands: A1LVR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function KCNQ2_HUMAN Publication Abstract from PubMed 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(2)) 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(2) 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. Structure basis for the activation of KCNQ2 by endogenous and exogenous ligands.,Zhao Y, Yang Z, Shi S, Hao H, Li X, Ma D, Su N, Zhao W, Shao J, An Y, Wang K, Liu Y, Zou L, Qi J, Zhang H, Guo J, Du X Cell Rep. 2026 Jan 27;45(1):116771. doi: 10.1016/j.celrep.2025.116771. Epub 2025 , Dec 23. PMID:41442279 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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