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Curr Opin Struct Biol. 2019 Aug 1. pii: S0959-440X(19)30066-1. doi: 10.1016/j.sbi.2019.06.011. [Epub ahead of print]

The role of π-helices in TRP channel gating.

Author information

1
Department of Biochemistry, Duke University School of Medicine, Durham, NC, 27710, USA.
2
Department of Biochemistry, Duke University School of Medicine, Durham, NC, 27710, USA. Electronic address: seok-yong.lee@duke.edu.

Abstract

Transient Receptor Potential (TRP) channels are a large superfamily of polymodal ion channels, which perform important roles in numerous physiological processes. The architecture of their transmembrane (TM) domains closely resembles that of voltage-gated potassium channels (KV). However, recent cryoEM and crystallographic studies of TRP channels have identified π-helices in functionally important regions, and it is increasingly recognized that they utilize a distinct mechanism of gating that relies on α-to-π secondary structure transitions. Here we review our current understanding of the role of π-helices in TRP channel function and their broader impact on different classes of ion channels.

PMID:
31378426
DOI:
10.1016/j.sbi.2019.06.011

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