Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Activation and closed-state inactivation mechanisms of the human voltage-gated K4 channel complexes.
Journal, issue, pages	Mol Cell, Vol. 82, Issue 13, Page 2427-22442.e4, Year 2022
Publish date	Jul 7, 2022
Authors	Wenlei Ye / Hongtu Zhao / Yaxin Dai / Yingdi Wang / Yu-Hua Lo / Lily Yeh Jan / Chia-Hsueh Lee /
PubMed Abstract	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 ...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 links	Mol Cell / PubMed:35597238 / PubMed Central
Methods	EM (single particle)
Resolution	2.24 - 3.02 Å
Structure data	26575 7uk5 EMDB-26575, PDB-7uk5: Human Kv4.2-KChIP2 channel complex in an open state, transmembrane region Method: EM (single particle) / Resolution: 2.76 Å 26576 7ukc 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 26577 7ukd 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 26578 7uke EMDB-26578, PDB-7uke: Human Kv4.2-KChIP2 channel complex in an intermediate state, transmembrane region Method: EM (single particle) / Resolution: 3.01 Å 26579 7ukf 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 26580 7ukg 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 26581 7ukh 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)
Keywords	TRANSPORT PROTEIN / potassium channel complex / MEMBRANE PROTEIN