Crystal structure of an inactivated mutant mammalian voltage-gated K⁺ channel.

ABSTRACT: C-type inactivation underlies important roles played by voltage-gated K⁺ (Kv) channels. Functional studies have provided strong evidence that a common underlying cause of this type of inactivation is an alteration near the extracellular end of the channel's ion-selectivity filter. Unlike N-type inactivation, which is known to reflect occlusion of the channel's intracellular end, the structural mechanism of C-type inactivation remains controversial and may have many detailed variations. Here we report that in voltage-gated Shaker K⁺ channels lacking N-type inactivation, a mutation enhancing inactivation disrupts the outermost K⁺ site in the selectivity filter. Furthermore, in a crystal structure of the Kv1.2-2.1 chimeric channel bearing the same mutation, th

SUBMITTER: Pau V 

PROVIDER: S-EPMC5652298 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature