Global alignment and assessment of TRP channel transmembrane domain structures to explore functional mechanisms.

ABSTRACT: The recent proliferation of published TRP channel structures provides a foundation for understanding the diverse functional properties of this important family of ion channel proteins. To facilitate mechanistic investigations, we constructed a structure-based alignment of the transmembrane domains of 120 TRP channel structures. Comparison of structures determined in the absence or presence of activating stimuli reveals similar constrictions in the central ion permeation pathway near the intracellular end of the S6 helices, pointing to a conserved cytoplasmic gate and suggesting that most available structures represent non-conducting states. Comparison of the ion selectivity filters toward the extracellular end of the pore supports existing hypotheses for mechanisms of ion selectivity. Also

SUBMITTER: Huffer KE 

PROVIDER: S-EPMC7431192 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature