6BO4

Open state structure of the full-length TRPV2 cation channel with a resolved pore turret domain

Summary for 6BO4

• Entry DOI: 10.2210/pdb6bo4/pdb
• Related: 6BO5
• EMDB information: 7118 7119
• Descriptor: Transient receptor potential cation channel subfamily V member 2 (1 entity in total)
• Functional Keywords: channel, trp, cation, open, membrane protein
• Biological source: Rattus norvegicus (Rat)
• Total number of polymer chains: 4
• Total formula weight: 319997.69

Authors

Dosey, T.L.,Wang, Z. (deposition date: 2017-11-18, release date: 2018-12-05, Last modification date: 2025-05-28)

Primary citation

Dosey, T.L.,Wang, Z.,Fan, G.,Zhang, Z.,Serysheva, I.I.,Chiu, W.,Wensel, T.G.
Structures of TRPV2 in distinct conformations provide insight into role of the pore turret.
Nat.Struct.Mol.Biol., 26:40-49, 2019

PubMed Abstract: Cation channels of the transient receptor potential (TRP) family serve important physiological roles by opening in response to diverse intra- and extracellular stimuli that regulate their lower or upper gates. Despite extensive studies, the mechanism coupling these gates has remained obscure. Previous structures have failed to resolve extracellular loops, known in the TRPV subfamily as 'pore turrets', which are proximal to the upper gates. We established the importance of the pore turret through activity assays and by solving structures of rat TRPV2, both with and without an intact turret at resolutions of 4.0 Å and 3.6 Å, respectively. These structures resolve the full-length pore turret and reveal fully open and partially open states of TRPV2, both with unoccupied vanilloid pockets. Our results suggest a mechanism by which physiological signals, such as lipid binding, can regulate the lower gate and couple to the upper gate through a pore-turret-facilitated mechanism.

PubMed: 30598551
DOI: 10.1038/s41594-018-0168-8

Experimental method

ELECTRON MICROSCOPY (4 Å)