Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7LQY

Structure of squirrel TRPV1 in apo state

Summary for 7LQY
Entry DOI10.2210/pdb7lqy/pdb
EMDB information23491
DescriptorOsm-9-like TRP channel 1, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate, 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoinositol, ... (5 entities in total)
Functional Keywordstransient receptor potential v family member 1, trp channel, trpv1 full length, trpv1 wild type, membrane protein
Biological sourceIctidomys tridecemlineatus (Thirteen-lined ground squirrel, Spermophilus tridecemlineatus)
Total number of polymer chains4
Total formula weight411340.27
Authors
Nadezhdin, K.D.,Neuberger, A.,Sobolevsky, A.I. (deposition date: 2021-02-15, release date: 2021-04-21, Last modification date: 2024-03-06)
Primary citationNadezhdin, K.D.,Neuberger, A.,Nikolaev, Y.A.,Murphy, L.A.,Gracheva, E.O.,Bagriantsev, S.N.,Sobolevsky, A.I.
Extracellular cap domain is an essential component of the TRPV1 gating mechanism.
Nat Commun, 12:2154-2154, 2021
Cited by
PubMed Abstract: Transient receptor potential (TRP) channels are polymodal molecular sensors involved in numerous physiological processes and implicated in a variety of human diseases. Several structures of the founding member of the TRP channel family, TRPV1, are available, all of which were determined for the protein missing the N- and C-termini and the extracellular S5-P-loop. Here, we present structures of the full-length thirteen-lined ground squirrel TRPV1 solved by cryo-EM. Our structures resolve the extracellular cap domain formed by the S5-P-loops and the C-terminus that wraps around the three-stranded β-sheet connecting elements of the TRPV1 intracellular skirt. The cap domain forms a dome above the pore's extracellular entrance, with four portals leading to the ion conductance pathway. Deletion of the cap increases the TRPV1 average conductance, reduces the open probability and affects ion selectivity. Our data show that both the termini and the cap domain are critical determinants of TRPV1 function.
PubMed: 33846324
DOI: 10.1038/s41467-021-22507-3
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.19 Å)
Structure validation

227561

PDB entries from 2024-11-20

PDB statisticsPDBj update infoContact PDBjnumon