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TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action.

<div class='caption-title'>TRPV1 structures determined in lipid nanodisc</div>
<div class='caption-title'>Structural details of tripartite toxin-channel-lipid complex</div>
<div class='caption-title'>Movement of protein and lipids associated with toxin binding</div>
Gao Y, Cao E, Julius D, Cheng Y
OpenAccess logo Nature 534 347-51 (2016)
Related entries: 5irz, 5is0

Cited: 454 times
EuropePMC logo PMID: 27281200

Abstract

When integral membrane proteins are visualized in detergents or other artificial systems, an important layer of information is lost regarding lipid interactions and their effects on protein structure. This is especially relevant to proteins for which lipids have both structural and regulatory roles. Here we demonstrate the power of combining electron cryo-microscopy with lipid nanodisc technology to ascertain the structure of the rat TRPV1 ion channel in a native bilayer environment. Using this approach, we determined the locations of annular and regulatory lipids and showed that specific phospholipid interactions enhance binding of a spider toxin to TRPV1 through formation of a tripartite complex. Furthermore, phosphatidylinositol lipids occupy the binding site for capsaicin and other vanilloid ligands, suggesting a mechanism whereby chemical or thermal stimuli elicit channel activation by promoting the release of bioactive lipids from a critical allosteric regulatory site.

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Articles - 5irx mentioned but not cited (43)



Reviews citing this publication (124)

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