Journal
CELL
Volume 141, Issue 5, Pages 834-845Publisher
CELL PRESS
DOI: 10.1016/j.cell.2010.03.052
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Funding
- National Institutes of Health (NIH) National Center for Research Resources
- NIH/National Institute of Neurological Disorders and Stroke (NINDS)
- Damon Runyon Cancer Research Foundation
- International Human Frontier Science Program Organization
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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.
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