6PVL
Cryo-EM structure of mouse TRPV3 in closed state at 42 degrees Celsius
Summary for 6PVL
Entry DOI | 10.2210/pdb6pvl/pdb |
EMDB information | 20492 20493 20494 20495 20496 20497 |
Descriptor | Transient receptor potential cation channel subfamily V member 3, SODIUM ION (2 entities in total) |
Functional Keywords | ion channels, membrane protein, trp channels, transport protein |
Biological source | Mus musculus (Mouse) |
Total number of polymer chains | 4 |
Total formula weight | 370568.76 |
Authors | Singh, A.K.,McGoldrick, L.L.,Sobolevsky, A.I. (deposition date: 2019-07-21, release date: 2019-10-23, Last modification date: 2024-03-20) |
Primary citation | Singh, A.K.,McGoldrick, L.L.,Demirkhanyan, L.,Leslie, M.,Zakharian, E.,Sobolevsky, A.I. Structural basis of temperature sensation by the TRP channel TRPV3. Nat.Struct.Mol.Biol., 26:994-998, 2019 Cited by PubMed Abstract: We present structures of mouse TRPV3 in temperature-dependent open, closed and intermediate states that suggest two-step activation of TRPV3 by heat. During the strongly temperature-dependent first step, sensitization, the channel pore remains closed while S6 helices undergo α-to-π transitions. During the weakly temperature-dependent second step, channel opening, tight association of the S1-S4 and pore domains is stabilized by changes in the carboxy-terminal and linker domains. PubMed: 31636415DOI: 10.1038/s41594-019-0318-7 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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