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5IRZ

Structure of TRPV1 determined in lipid nanodisc

Summary for 5IRZ
Entry DOI10.2210/pdb5irz/pdb
Related5IRX 5IS0
EMDB information5778 8117 8118 8119 8120
DescriptorTransient receptor potential cation channel subfamily V member 1, (4R,7S)-4-hydroxy-N,N,N-trimethyl-4,9-dioxo-7-[(pentanoyloxy)methyl]-3,5,8-trioxa-4lambda~5~-phosphatetradecan-1-aminium, (2S)-1-{[(R)-hydroxy{[(1R,2R,3S,4S,5S,6S)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}-3-(pentanoyloxy)propan-2-yl decanoate, ... (4 entities in total)
Functional Keywordstrp, ion channel, nanodisc, vanilloid, lipid, transport protein
Biological sourceRattus norvegicus (Rat)
More
Total number of polymer chains4
Total formula weight302472.31
Authors
Gao, Y.,Cao, E.,Julius, D.,Cheng, Y. (deposition date: 2016-03-15, release date: 2016-05-25, Last modification date: 2024-03-06)
Primary citationGao, Y.,Cao, E.,Julius, D.,Cheng, Y.
TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action.
Nature, 534:347-351, 2016
Cited by
PubMed 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.
PubMed: 27281200
DOI: 10.1038/nature17964
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.28 Å)
Structure validation

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