Structural highlights
FunctionKCAB2_RAT Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Publication Abstract from PubMedC-type inactivation is a process by which ion flux through a voltage-gated K(+) (K(v)) 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 K(v)1.2 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. Structural basis for C-type inactivation in a Shaker family voltage-gated K(+) channel.,Reddi R, Matulef K, Riederer EA, Whorton MR, Valiyaveetil FI Sci Adv. 2022 Apr 22;8(16):eabm8804. doi: 10.1126/sciadv.abm8804. Epub 2022 Apr , 22. PMID:35452285[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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