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2018 ; 12
(1
): 137-152
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X-ray crystallography of TRP channels
#MMPMID29589513
Singh AK
; McGoldrick LL
; Saotome K
; Sobolevsky AI
Channels (Austin)
2018[Jan]; 12
(1
): 137-152
PMID29589513
show ga
Transient receptor potential (TRP) ion channels are molecular sensors of a large
variety of stimuli including temperature, mechanical stress, voltage, small
molecules including capsaicin and menthol, and lipids such as
phosphatidylinositol 4,5-bisphosphate (PIP(2)). Since the same TRP channels may
respond to different physical and chemical stimuli, they can serve as signal
integrators. Many TRP channels are calcium permeable and contribute to Ca(2+)
homeostasis and signaling. Although the TRP channel family was discovered decades
ago, only recently have the structures of many of these channels been solved,
largely by cryo-electron microscopy (cryo-EM). Complimentary to cryo-EM, X-ray
crystallography provides unique tools to unambiguously identify specific atoms
and can be used to study ion binding in channel pores. In this review we describe
crystallographic studies of the TRP channel TRPV6. The methodology used in these
studies may serve as a template for future structural analyses of different types
of TRP and other ion channels.