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Structure paper

TitleTRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action.
Journal, issue, pagesNature, Vol. 534, Issue 7607, Page 347-351, Year 2016
Publish dateJun 16, 2016
AuthorsYuan Gao / Erhu Cao / David Julius / Yifan Cheng /
PubMed AbstractWhen 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. ...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.
External linksNature / PubMed:27281200 / PubMed Central
MethodsEM (single particle)
Resolution2.95 - 3.8 Å
Structure data

8117

5irx

EMDB-8117, PDB-5irx:
Structure of TRPV1 in complex with DkTx and RTX, determined in lipid nanodisc
Method: EM (single particle) / Resolution: 2.95 Å

8118

5irz

EMDB-8118, PDB-5irz:
Structure of TRPV1 determined in lipid nanodisc
Method: EM (single particle) / Resolution: 3.28 Å

8119

5is0

EMDB-8119, PDB-5is0:
Structure of TRPV1 in complex with capsazepine, determined in lipid nanodisc
Method: EM (single particle) / Resolution: 3.43 Å

EMDB-8120:
Structure of TRPV1 in complex with capsazepine, determined in lipid nanodisc
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-6O8:
(4R,7S)-4-hydroxy-N,N,N-trimethyl-4,9-dioxo-7-[(pentanoyloxy)methyl]-3,5,8-trioxa-4lambda~5~-phosphatetradecan-1-aminium

ChemComp-6OE:
(2S)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(hexanoyloxy)propyl hexanoate

ChemComp-6EU:
resiniferatoxin / toxin*YM / Resiniferatoxin

ChemComp-6O9:
(2S)-2-(acetyloxy)-3-{[(R)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}propyl pentanoate

ChemComp-6ES:
(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

ChemComp-6ET:
capsazepine / antagonist*YM / Capsazepine

Source
  • rattus norvegicus (Norway rat)
  • haplopelma schmidti (Chinese earth tiger)
KeywordsTRANSPORT PROTEIN / TRP / ion channel / nanodisc / vanilloid / lipid / interaction

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