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Journal article

Engineering vanilloid-sensitivity into the rat TRPV2 channel.

Abstract:

The TRPV1 channel is a detector of noxious stimuli, including heat, acidosis, vanilloid compounds and lipids. The gating mechanisms of the related TRPV2 channel are poorly understood because selective high affinity ligands are not available, and the threshold for heat activation is extremely high (> 50 {degree sign}C). Cryo-EM structures of TRPV1 and TRPV2 reveal that they adopt similar structures, and identify a putative vanilloid binding pocket near the internal side of TRPV1. Here we us...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.7554/eLife.16409

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
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Name:
Wellcome Trust
Funding agency for:
Newstead, S
Grant:
102890/Z/13/Z
Publisher:
eLife Sciences Publications
Journal:
eLife More from this journal
Volume:
5
Publication date:
2016-05-13
Acceptance date:
2016-05-12
DOI:
EISSN:
2050-084X
Language:
English
Keywords:
Pubs id:
pubs:623112
UUID:
uuid:24b3f21c-e121-4ebe-8256-7a7d0ea9056e
Local pid:
pubs:623112
Source identifiers:
623112
Deposit date:
2016-05-23

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