TRPV2 ion channel gating through allosteric domain coupling revealed by cryo-EM
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ABSTRACT:
SUBMITTER: TG Wensel
PROVIDER: EMPIAR-10247 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structures of TRPV2 in distinct conformations provide insight into role of the pore turret.
Dosey Timothy L TL Wang Zhao Z Fan Guizhen G Zhang Zhixian Z Serysheva Irina I II Chiu Wah W Wensel Theodore G TG
Nature structural & molecular biology 20181231 1
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 ...[more]
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