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Significance After opening in response to a specific stimulus, some potassium channels undergo C-type inactivation. Crystal structures of KcsA have revealed that the selectivity filter constricts under conditions associated with C-type inactivation. Functional studies based on semisynthetic KcsA channels with either D-ala77 or amide-to-ester backbone substitutions provide important observations arguing against the constricted conformation of the selectivity filter as the molecular basis of C-type inactivation. In this study, molecular dynamics simulations based on atomic models of the KcsA channel are performed to clarify the impact of these chemical modifications on the conformation of the selectivity filter. The results support the notion that the constricted conformation of the selectivity filter, indeed, corresponds to the functional C-type inactivated state of the KcsA channel.

Chemical substitutions in the selectivity filter of potassium channels do not rule out constricted-like conformations for C-type inactivation