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PDBsum entry 5irz
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Transport protein
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PDB id
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5irz
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PDB id:
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| Name: |
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Transport protein
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Title:
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Structure of trpv1 determined in lipid nanodisc
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Structure:
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Transient receptor potential cation channel subfamily v member 1. Chain: d, e, b, c. Fragment: unp residues 110-603, 627-764. Synonym: trpv1, capsaicin receptor, osm-9-like trp channel 1, otrpc1, vanilloid receptor 1, vanilloid receptor type 1-like. Engineered: yes
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Source:
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Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: trpv1, vr1, vr1l. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek 293s
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Authors:
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Y.Gao,E.Cao,D.Julius,Y.Cheng
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Key ref:
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Y.Gao
et al.
(2016).
TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action.
Nature,
534,
347-351.
PubMed id:
DOI:
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Date:
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15-Mar-16
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Release date:
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25-May-16
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PROCHECK
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Headers
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References
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O35433
(TRPV1_RAT) -
Transient receptor potential cation channel subfamily V member 1 from Rattus norvegicus
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Seq:
Struc:
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838 a.a.
394 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Nature
534:347-351
(2016)
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PubMed id:
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TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action.
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Y.Gao,
E.Cao,
D.Julius,
Y.Cheng.
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ABSTRACT
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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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Links
