Journal article icon

Journal article

Activation mechanism of ATP-sensitive K+ channels explored with real-time nucleotide binding

Abstract:

The response of ATP-sensitive K+ channels (KATP) to cellular metabolism is coordinated by three classes of nucleotide binding site (NBS). We used a novel approach involving labeling of intact channels in a native, membrane environment with a non-canonical fluorescent amino acid and measurement (using FRET with fluorescent nucleotides) of steady-state and time-resolved nucleotide binding to dissect the role of NBS2 of the accessory SUR1 subunit of KATP in channel gating. Binding to NBS2 was Mg...

Expand abstract
Publication status:
Published
Peer review status:
Peer reviewed

Actions


Access Document


Files:
Publisher copy:
10.7554/eLife.41103

Authors


More by this author
Role:
Author
ORCID:
0000-0002-9335-0936
More by this author
Role:
Author
ORCID:
0000-0002-2487-6547
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Physiology Anatomy and Genetics
Oxford college:
Trinity College
Role:
Author
ORCID:
0000-0002-6970-1767
Publisher:
eLife Sciences Publisher's website
Journal:
eLife Journal website
Volume:
8
Issue:
2019
Article number:
e41103
Publication date:
2019-02-21
Acceptance date:
2019-02-14
DOI:
EISSN:
2050-084X
ISSN:
2050-084X
Pmid:
30789344
Language:
English
Keywords:
Pubs id:
pubs:980975
UUID:
uuid:6a9f7194-fe39-4c57-8dc9-f094863004f0
Local pid:
pubs:980975
Source identifiers:
980975
Deposit date:
2019-04-02

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP