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Structure paper

TitleStructural basis for the subtype-selectivity of K2.2 channel activators.
Journal, issue, pagesRes Sq, Year 2025
Publish dateMay 16, 2025
AuthorsMiao Zhang / Young-Woo Nam / Alena Ramanishka / Yang Xu / Rose Marie Yasuda / Dohyun Im / Meng Cui / George Chandy / Heike Wulff /
PubMed AbstractSmall-conductance (K2.2) and intermediate-conductance (K3.1) Ca-activated K channels are gated by a Ca-calmodulin dependent mechanism. NS309 potentiates the activity of both K2.2 and K3.1, while ...Small-conductance (K2.2) and intermediate-conductance (K3.1) Ca-activated K channels are gated by a Ca-calmodulin dependent mechanism. NS309 potentiates the activity of both K2.2 and K3.1, while rimtuzalcap selectively activates K2.2. Rimtuzalcap has been used in clinical trials for the treatment of spinocerebellar ataxia and essential tremor. We report cryo-electron microscopy structures of K2.2 channels bound with NS309 and rimtuzalcap, in addition to K3.1 channels with NS309. The different conformations of calmodulin and the cytoplasmic HC helices in the two channels underlie the subtype-selectivity of rimtuzalcap for K2.2. Calmodulin's N-lobes in the K2.2 structure are far apart and undergo conformational changes to accommodate either NS309 or rimtuzalcap. Calmodulin's Nlobes in the K3.1 structure are closer to each other and are constrained by the HC helices of K3.1, which allows binding of NS309 but not of the bulkier rimtuzalcap. These structures provide a framework for structure-based drug design targeting K2.2 channels.
External linksRes Sq / PubMed:40470184 / PubMed Central
MethodsEM (single particle)
Resolution2.71 - 3.59 Å
Structure data

70207

9o7s

EMDB-70207, PDB-9o7s:
Cryo-EM structure of KCa2.2/calmodulin channel in complex with NS309
Method: EM (single particle) / Resolution: 2.71 Å

70217

9o85

EMDB-70217, PDB-9o85:
Cryo-EM structure of KCa2.2_I/calmodulin channel in complex with rimtuzalcap
Method: EM (single particle) / Resolution: 3.13 Å

70240

9o93

EMDB-70240, PDB-9o93:
Cryo-EM structure of KCa2.2_II/calmodulin channel in complex with rimtuzalcap
Method: EM (single particle) / Resolution: 2.96 Å

70275

9oa8

EMDB-70275, PDB-9oa8:
Cryo-EM structure of KCa3.1/calmodulin channel in complex with NS309
Method: EM (single particle) / Resolution: 3.59 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-1KP:
(3E)-6,7-dichloro-3-(hydroxyimino)-1,3-dihydro-2H-indol-2-one

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

PDB-1b92:
MOBILITY OF AN HIV-1 INTEGRASE ACTIVE SITE LOOP IS CORRELATED WITH CATALYTIC ACTIVITY

Source
  • rattus norvegicus (Norway rat)
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Ion channel / Small-conductance calcium-activated potassium channel / Membrane protein / Intermediate conductance calcium-activated potassium channel / Calmodulin binding protein

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