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A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain

Item Type:Article
Title:A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain
Creators Name:Bohlen, C.J. and Priel, A. and Zhou, S. and King, D. and Siemens, J. and Julius, D.
Abstract:Toxins have evolved to target regions of membrane ion channels that underlie ligand binding, gating, or ion permeation, and have thus served as invaluable tools for probing channel structure and function. Here, we describe a peptide toxin from the Earth Tiger tarantula that selectively and irreversibly activates the capsaicin- and heat-sensitive channel, TRPV1. This high-avidity interaction derives from a unique tandem repeat structure of the toxin that endows it with an antibody-like bivalency. The "double-knot" toxin traps TRPV1 in the open state by interacting with residues in the presumptive pore-forming region of the channel, highlighting the importance of conformational changes in the outer pore region of TRP channels during activation
Keywords:MOLNEURO, SIGNALING, PROTEINS, Animals, Rats
Source:Cell
ISSN:0092-8674
Publisher:Cell Press (U.S.A.)
Volume:141
Number:5
Page Range:834-845
Date:28 May 2010
Official Publication:https://doi.org/10.1016/j.cell.2010.03.052
PubMed:View item in PubMed

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