cad 1883 Search Results


cad 1883  (MedChemExpress)
94
MedChemExpress cad 1883
a Chemical structure of <t>CAD-1883.</t> b Concentration-dependent activation curve of SK2 by CAD-1883. Representative whole-cell current traces of SK2 enhanced by CAD-1883. Voltage ramp, -100 mV to 100 mV (Left). Data are presented as mean values ± SEM ( n = 8 cells). Curve was fitted using nonlinear regression. c Cryo-EM density map of CAD-1883 in SK2-CAD-1883 complex. Density maps for CAD-1883 and interacting residues are shown in purple and gray meshes, respectively. d Detailed interactions between CAD-1883 and SK2-CaM complex. CAD-1883 in cyan sticks, residues involved in CAD-1883 binding are shown in sticks. e – h CAD-1883 stimulated current traces of WT SK2 ( e ), L291W ( f ), L291F (g), and LN291-292AA ( h ). The free Ca 2+ concentration in the internal solution is 300 nM. CAD-1883 is applied to the external solution at 100 μM. i Pore radius analysis of SK2-apamin and SK2-CAD-1883 by HOLE. Two opposing subunits are shown as cartoons; pores of SK2-apamin and SK2-CAD-1883 are shown as pink and yellow, respectively. j Pore radius profiles of SK2-apamin and SK2-CAD-1883 along the pore axis. Selectivity filter (SF) and activation gate (AG) regions are shaded in pink and light blue. k Superposition of SK2-CAD-1883 (cyan) and opened SK4 (gray, PDB: 6cno). Black arrows indicate conformational changes. Source Data are provided as a Source Data file.
Cad 1883, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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a Chemical structure of CAD-1883. b Concentration-dependent activation curve of SK2 by CAD-1883. Representative whole-cell current traces of SK2 enhanced by CAD-1883. Voltage ramp, -100 mV to 100 mV (Left). Data are presented as mean values ± SEM ( n = 8 cells). Curve was fitted using nonlinear regression. c Cryo-EM density map of CAD-1883 in SK2-CAD-1883 complex. Density maps for CAD-1883 and interacting residues are shown in purple and gray meshes, respectively. d Detailed interactions between CAD-1883 and SK2-CaM complex. CAD-1883 in cyan sticks, residues involved in CAD-1883 binding are shown in sticks. e – h CAD-1883 stimulated current traces of WT SK2 ( e ), L291W ( f ), L291F (g), and LN291-292AA ( h ). The free Ca 2+ concentration in the internal solution is 300 nM. CAD-1883 is applied to the external solution at 100 μM. i Pore radius analysis of SK2-apamin and SK2-CAD-1883 by HOLE. Two opposing subunits are shown as cartoons; pores of SK2-apamin and SK2-CAD-1883 are shown as pink and yellow, respectively. j Pore radius profiles of SK2-apamin and SK2-CAD-1883 along the pore axis. Selectivity filter (SF) and activation gate (AG) regions are shaded in pink and light blue. k Superposition of SK2-CAD-1883 (cyan) and opened SK4 (gray, PDB: 6cno). Black arrows indicate conformational changes. Source Data are provided as a Source Data file.

Journal: Nature Communications

Article Title: Structural mechanisms for inhibition and activation of human small-conductance Ca 2+ -activated potassium channel SK2

doi: 10.1038/s41467-026-68475-4

Figure Lengend Snippet: a Chemical structure of CAD-1883. b Concentration-dependent activation curve of SK2 by CAD-1883. Representative whole-cell current traces of SK2 enhanced by CAD-1883. Voltage ramp, -100 mV to 100 mV (Left). Data are presented as mean values ± SEM ( n = 8 cells). Curve was fitted using nonlinear regression. c Cryo-EM density map of CAD-1883 in SK2-CAD-1883 complex. Density maps for CAD-1883 and interacting residues are shown in purple and gray meshes, respectively. d Detailed interactions between CAD-1883 and SK2-CaM complex. CAD-1883 in cyan sticks, residues involved in CAD-1883 binding are shown in sticks. e – h CAD-1883 stimulated current traces of WT SK2 ( e ), L291W ( f ), L291F (g), and LN291-292AA ( h ). The free Ca 2+ concentration in the internal solution is 300 nM. CAD-1883 is applied to the external solution at 100 μM. i Pore radius analysis of SK2-apamin and SK2-CAD-1883 by HOLE. Two opposing subunits are shown as cartoons; pores of SK2-apamin and SK2-CAD-1883 are shown as pink and yellow, respectively. j Pore radius profiles of SK2-apamin and SK2-CAD-1883 along the pore axis. Selectivity filter (SF) and activation gate (AG) regions are shaded in pink and light blue. k Superposition of SK2-CAD-1883 (cyan) and opened SK4 (gray, PDB: 6cno). Black arrows indicate conformational changes. Source Data are provided as a Source Data file.

Article Snippet: To purify ligand-bound complexes, different ligands, including Apamin (MedChemExpress), UCL1684 (Merck), CAD-1883 (MedChemExpress) and AP30663 (MedChemExpress), were mixed with the SK2-CaM sample for at least 30 min, respectively.

Techniques: Concentration Assay, Activation Assay, Cryo-EM Sample Prep, Binding Assay

a When intracellular Ca 2+ is at low levels, the SK2 channel assumes a closed resting state. The C-lobe of CaM binds to the HA helix of SK2, while the N-lobe is dynamic. b After intracellular Ca 2+ increased to sub-micromolar levels, Ca 2+ ions bind to CaM N-lobe and induce conformational changes that facilitate the engagement of CaM N-lobe and the S 45 A helix, resulting in pore opening. c Multiple modulation sites in the SK2-CaM complex. Site 1 in the outer vestibule for apamin and UCL1684; Site 2 in the central cavity for AP30663 analogs; Site 3 in the CaM N-lobe and SK2 S 45 A helix interface for activators such as CAD-1883 and NS-309.

Journal: Nature Communications

Article Title: Structural mechanisms for inhibition and activation of human small-conductance Ca 2+ -activated potassium channel SK2

doi: 10.1038/s41467-026-68475-4

Figure Lengend Snippet: a When intracellular Ca 2+ is at low levels, the SK2 channel assumes a closed resting state. The C-lobe of CaM binds to the HA helix of SK2, while the N-lobe is dynamic. b After intracellular Ca 2+ increased to sub-micromolar levels, Ca 2+ ions bind to CaM N-lobe and induce conformational changes that facilitate the engagement of CaM N-lobe and the S 45 A helix, resulting in pore opening. c Multiple modulation sites in the SK2-CaM complex. Site 1 in the outer vestibule for apamin and UCL1684; Site 2 in the central cavity for AP30663 analogs; Site 3 in the CaM N-lobe and SK2 S 45 A helix interface for activators such as CAD-1883 and NS-309.

Article Snippet: To purify ligand-bound complexes, different ligands, including Apamin (MedChemExpress), UCL1684 (Merck), CAD-1883 (MedChemExpress) and AP30663 (MedChemExpress), were mixed with the SK2-CaM sample for at least 30 min, respectively.

Techniques: