6BWJ

Crystal structure of the TRPV2 ion channel in complex with RTx

Summary for 6BWJ

• Entry DOI: 10.2210/pdb6bwj/pdb
• Descriptor: Transient receptor potential cation channel subfamily V member 2, resiniferatoxin, CALCIUM ION (3 entities in total)
• Functional Keywords: ion channel, trpv channel, membrane protein, heat sensor, temperature sensing ion channel, ca2+ channel
• Biological source: Oryctolagus cuniculus (Rabbit)
• Total number of polymer chains: 2
• Total formula weight: 176548.38

Authors

Zubcevic, L.,Le, S.,Yang, H.,Lee, S.Y. (deposition date: 2017-12-15, release date: 2018-05-02, Last modification date: 2023-10-04)

Primary citation

Zubcevic, L.,Le, S.,Yang, H.,Lee, S.Y.
Conformational plasticity in the selectivity filter of the TRPV2 ion channel.
Nat. Struct. Mol. Biol., 25:405-415, 2018

PubMed Abstract: Transient receptor potential vanilloid (TRPV) channels are activated by ligands and heat and are involved in various physiological processes. In contrast to the architecturally related voltage-gated cation channels, TRPV1 and TRPV2 subtypes possess another activation gate at the selectivity filter that can open widely enough to permeate large organic cations. Despite recent structural advances, the mechanism of selectivity filter gating and permeation for both metal ions and large molecules by TRPV1 or TRPV2 is not well known. Here, we determined two crystal structures of rabbit TRPV2 in its Ca-bound and resiniferatoxin (RTx)- and Ca-bound forms, to 3.9 Å and 3.1 Å, respectively. Notably, our structures show that RTx binding leads to two-fold symmetric opening of the selectivity filter of TRPV2 that is wide enough for large organic cation permeation. Combined with functional characterizations, our studies reveal a structural basis for permeation of Ca and large organic cations in TRPV2.

PubMed: 29728656
DOI: 10.1038/s41594-018-0059-z

Experimental method

X-RAY DIFFRACTION (3.1 Å)