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TitleActivation and closed-state inactivation mechanisms of the human voltage-gated K4 channel complexes.
Journal, issue, pagesMol Cell, Vol. 82, Issue 13, Page 2427-22442.e4, Year 2022
Publish dateJul 7, 2022
AuthorsWenlei Ye / Hongtu Zhao / Yaxin Dai / Yingdi Wang / Yu-Hua Lo / Lily Yeh Jan / Chia-Hsueh Lee /
PubMed AbstractThe voltage-gated ion channel activity depends on both activation (transition from the resting state to the open state) and inactivation. Inactivation is a self-restraint mechanism to limit ion ...The voltage-gated ion channel activity depends on both activation (transition from the resting state to the open state) and inactivation. Inactivation is a self-restraint mechanism to limit ion conduction and is as crucial to membrane excitability as activation. Inactivation can occur when the channel is open or closed. Although open-state inactivation is well understood, the molecular basis of closed-state inactivation has remained elusive. We report cryo-EM structures of human K4.2 channel complexes in inactivated, open, and closed states. Closed-state inactivation of K4 involves an unprecedented symmetry breakdown for pore closure by only two of the four S4-S5 linkers, distinct from known mechanisms of open-state inactivation. We further capture K4 in a putative resting state, revealing how voltage sensor movements control the pore. Moreover, our structures provide insights regarding channel modulation by KChIP2 and DPP6 auxiliary subunits. Our findings elucidate mechanisms of closed-state inactivation and voltage-dependent activation of the K4 channel.
External linksMol Cell / PubMed:35597238 / PubMed Central
MethodsEM (single particle)
Resolution2.24 - 3.02 Å
Structure data

EMDB-26575, PDB-7uk5:
Human Kv4.2-KChIP2 channel complex in an open state, transmembrane region
Method: EM (single particle) / Resolution: 2.76 Å

EMDB-26576, PDB-7ukc:
Human Kv4.2-KChIP2 channel complex in an inactivated state, class 1, transmembrane region
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-26577, PDB-7ukd:
Human Kv4.2-KChIP2 channel complex in an inactivated state, class 2, transmembrane region
Method: EM (single particle) / Resolution: 2.88 Å

EMDB-26578, PDB-7uke:
Human Kv4.2-KChIP2 channel complex in an intermediate state, transmembrane region
Method: EM (single particle) / Resolution: 3.01 Å

EMDB-26579, PDB-7ukf:
Human Kv4.2-KChIP2 channel complex in a putative resting state, transmembrane region
Method: EM (single particle) / Resolution: 3.02 Å

EMDB-26580, PDB-7ukg:
Human Kv4.2-KChIP2-DPP6 channel complex in an open state, transmembrane region
Method: EM (single particle) / Resolution: 2.24 Å

EMDB-26581, PDB-7ukh:
Human Kv4.2-KChIP2-DPP6 channel complex in an open state, intracellular region
Method: EM (single particle) / Resolution: 2.33 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-HG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / potassium channel complex / MEMBRANE PROTEIN

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