Ask about this productRelated genes to: KCNN2 Blocking Peptide
- Gene:
- KCNN2 NIH gene
- Name:
- potassium calcium-activated channel subfamily N member 2
- Previous symbol:
- -
- Synonyms:
- KCa2.2, hSK2
- Chromosome:
- 5q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-04-07
- Date modifiied:
- 2016-02-04
Related products to: KCNN2 Blocking Peptide
Related articles to: KCNN2 Blocking Peptide
- Pathogenic variants in have previously been associated with X-linked intellectual disability and X-linked dystonia-parkinsonism. Epilepsy is observed in approximately 24.4% of affected individuals, ranging from focal seizures to generalized seizures including either tonic-clonic, tonic, myoclonic, atonic or absences. To date, no cases of infantile epileptic spasm syndrome (IESS) have been associated with this neurogenetic condition. In this study, we are aimed at investigating the association between and IESS. - Source: PubMed
Publication date: 2026/09/16
Xiao HuiXie ChangningPeng PanNi XiaoyuanMao LeileiPeng Jing - The K2.2 and K3.1 channels are fundamental regulators of membrane potential and calcium signalling and promising targets to treat diseases such as spinocerebellar ataxia and cancer. To fully exploit their therapeutic potential, and to continue studying their pathophysiological role, it is crucial to develop selective modulators for each of these two channels. Here, we present a computational study to identify the molecular determinants behind the selectivity of two recently reported K2.2 modulators, namely, N-(2,1,3-benzoxadiazol-4-yl)-3-(4-methoxybenzene-1-sulfonamido)benzamide and N-(2,1,3-benzoxadiazol-4-yl)-4-(trifluoromethyl)benzamide. We leveraged a protocol combining in silico mutagenesis, molecular dynamics simulations, and protein-ligand docking to analyse the pockets targeted by these ligands. We identified the Ser353/Pro245 substitution to be the main driver of the distinct pocket shapes in K2.2 and K3.1 channels, ultimately defining modulator selectivity. This approach provides novel insights into the structural differences of this binding site across potassium channel subtypes, proposing potential selectivity determinants of the modulators targeting this pocket. - Source: PubMed
Gozzi MatteoMassa JoanaKoch Oliver - Small-conductance Ca-activated potassium channels (SK) are increasingly investigated as therapeutic targets for atrial fibrillation. Emerging evidence, however, indicates their functional relevance in ventricular pathologies. This study investigates the expression, localization, and functional role of SK2 and SK3 channel subtypes in ventricular myocardium from patients with and without valvular disease-associated remodeling. - Source: PubMed
Publication date: 2026/07/07
Pérez-Martínez AlbaLópez-Andrés CristinaGarcía-Mendívil LauraLópez-Yus MartaBatín DianaVallejo-Gil Jose MFañanás-Mastral JavierVázquez-Sancho ManuelMatamala-Adell MartaSorribas-Berjón Juan FBellido-Morales Javier ABallester-Cuenca CarlosArbonés Mainar Jose MPueyo EstherOliván-Viguera Aída - Small-conductance Ca2+-activated K+ (SK) channels regulate neuronal excitability and act as a feedback mechanism to limit firing during sustained stimulation. In the present study, we demonstrated that SK2 plays an important role in the control of bladder function and visceral pain processing. SK2 channels are expressed in bladder-innervating afferent neurons, and ablation of this subunit results in elevated afferent firing rates in response to physiological levels of bladder distension, supporting a role for SK2 in modulating mechanosensory excitability. Mice overexpressing SK2 exhibit increased bladder capacity and reduced voiding frequency. Furthermore, overexpression of SK2 prevents the onset of pelvic mechanical allodynia and attenuates the exaggerated visceromotor response to bladder distension seen in wild-type mice with chemical cystitis. Thus, SK2 may be a promising target for treating overactive bladder and pain originating from the urinary bladder and other pelvic organs. - Source: PubMed
Publication date: 2026/05/22
Manrique-Maldonado GuadalupeSun XuejiaoMarciszyn Allison LMontalbetti NicolasCarattino Marcelo D - The intermediate-conductance (K3.1) and the small-conductance (K2.2) Ca-activated K channels share a Ca-calmodulin dependent gating mechanism. We report cryo-electron microscopy structures of K3.1 and K2.2 in complex with two benzothiazole-type activators. While SKA-31 is only moderately selective (∼7.3-fold), its derivative SKA-111 exhibits ∼70-fold selectivity for K3.1 over K2.2. SKA-31 and SKA-111 both bind in a pocket at the interface between the SA helix and calmodulin where they allosterically modulate the inner gate of the two channels. SKA-31 binds with comparable energies in the two channels, consistent with its moderate selectivity for K3.1 over K2.2. In the K3.1 structure, the calmodulin helix IV is positioned outward, forming a pocket that more readily accommodates the bulkier SKA-111 that sits deeper inside calmodulin's N-lobe in K3.1 than in K2.2. The resulting higher binding energy explains the improved selectivity of SKA-111 for K3.1 compared to the less selective SKA-31. - Source: PubMed
Publication date: 2026/05/14
Ramanishka AlenaNasburg Joshua AXu YangMa XinyiMehvar RezaCui MengNam Young-WooWulff HeikeZhang Miao