A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V.

ABSTRACT: C-type inactivation is of great physiological importance in voltage-activated K⁺ channels (Kv), but its structural basis remains unresolved. Knowledge about C-type inactivation has been largely deduced from the bacterial K⁺ channel KcsA, whose selectivity filter constricts under inactivating conditions. However, the filter is highly sensitive to its molecular environment, which is different in Kv channels than in KcsA. In particular, a glutamic acid residue at position 71 along the pore helix in KcsA is substituted by a valine conserved in most Kv channels, suggesting that this side chain is a molecular determinant of function. Here, a combination of X-ray crystallography, solid-state NMR and MD simulations of the E71V KcsA mutant is undertaken to explore inactivation

SUBMITTER: Rohaim A 

PROVIDER: S-EPMC8943062 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature