Dynamic molecular portraits of ion-conducting pores characterize functional states of TRPV channels.

ABSTRACT: Structural biology is solving an ever-increasing number of snapshots of ion channel conformational ensembles. Deciphering ion channel mechanisms, however, requires understanding the ensemble dynamics beyond the static structures. Here, we present a molecular modeling-based approach characterizing the ion channel structural intermediates, or their "dynamic molecular portraits", by assessing water and ion conductivity along with the detailed evaluation of pore hydrophobicity and residue packing. We illustrate the power of this approach by analyzing structures of few vanilloid-subfamily transient receptor potential (TRPV) channels. Based on the pore architecture, there are three major states that are common for TRPVs, which we call α-closed, π-closed, and π-open. We show that the pore hydroph

SUBMITTER: Trofimov YA 

PROVIDER: S-EPMC11144267 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature