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@article{Tzakoniati:2020:10.1016/j.chembiol.2019.10.011,
author = {Tzakoniati, F and Xu, H and Garcia, N and Kugel, C and Payandeh, J and Koth, CM and Tate, E},
doi = {10.1016/j.chembiol.2019.10.011},
journal = {Cell Chemical Biology},
pages = {306--313.e4},
title = {Development of photocrosslinking probes based on Huwentoxin-IV to map the site of interaction on Nav1.7},
url = {http://dx.doi.org/10.1016/j.chembiol.2019.10.011},
volume = {27},
year = {2020}
}
TY - JOUR
AB - Voltage-gated sodium (Nav) channels respond to changes in the membrane potential of excitable cells through the concerted action of four voltage-sensor domains (VSDs). Subtype Nav1.7 plays an important role in the propagation of signals in pain-sensing neurons and is a target for the clinical development of novel analgesics. Certain inhibitory cystine knot (ICK) peptides produced by venomous animals potently modulate Nav1.7, however the molecular mechanisms underlying their selective binding and activity remain elusive. This study reports on the design of a library of photoprobes based on the potent spider toxin Huwentoxin-IV and the determination of the toxin binding interface on VSD2 of Nav1.7 through a photocrosslinking and tandem mass spectrometry approach. Our Huwentoxin-IV probes selectively crosslink to extracellular loop S1-2 and helix S3 of VSD2 in a chimeric channel system. Our results provide a strategy that will enable mapping of sites of interaction of other ICK peptides on Nav channels.
AU - Tzakoniati,F
AU - Xu,H
AU - Garcia,N
AU - Kugel,C
AU - Payandeh,J
AU - Koth,CM
AU - Tate,E
DO - 10.1016/j.chembiol.2019.10.011
EP - 313
PY - 2020///
SN - 2451-9456
SP - 306
TI - Development of photocrosslinking probes based on Huwentoxin-IV to map the site of interaction on Nav1.7
T2 - Cell Chemical Biology
UR - http://dx.doi.org/10.1016/j.chembiol.2019.10.011
UR - https://www.sciencedirect.com/science/article/pii/S2451945619303563?via%3Dihub
UR - http://hdl.handle.net/10044/1/74682
VL - 27
ER -