7SIZ

C-type inactivation in a voltage gated K+ channel

Summary for 7SIZ

• Entry DOI: 10.2210/pdb7siz/pdb
• Descriptor: Voltage-gated potassium channel subunit beta-2, Voltage gated potassium channel Kv1.2-Kv2.1, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• Functional Keywords: voltage gated ion channel, c- type inactivation, beta subunit, transport protein, oxidoreductase
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 4
• Total formula weight: 194305.45

Authors

Reddi, R.,Riederer, E.A.,Matulef, K.,Whorton, M.R.,Valiyaveetil, F.I. (deposition date: 2021-10-15, release date: 2022-05-04, Last modification date: 2023-10-18)

Primary citation

Reddi, R.,Matulef, K.,Riederer, E.A.,Whorton, M.R.,Valiyaveetil, F.I.
Structural basis for C-type inactivation in a Shaker family voltage-gated K + channel.
Sci Adv, 8:eabm8804-eabm8804, 2022

PubMed Abstract: C-type inactivation is a process by which ion flux through a voltage-gated K (K) channel is regulated at the selectivity filter. While prior studies have indicated that C-type inactivation involves structural changes at the selectivity filter, the nature of the changes has not been resolved. Here, we report the crystal structure of the K1.2 channel in a C-type inactivated state. The structure shows that C-type inactivation involves changes in the selectivity filter that disrupt the outer two ion binding sites in the filter. The changes at the selectivity filter propagate to the extracellular mouth and the turret regions of the channel pore. The structural changes observed are consistent with the functional hallmarks of C-type inactivation. This study highlights the intricate interplay between K occupancy at the ion binding sites and the interactions of the selectivity filter in determining the balance between the conductive and the inactivated conformations of the filter.

PubMed: 35452285
DOI: 10.1126/sciadv.abm8804

Experimental method

X-RAY DIFFRACTION (3.1 Å)