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Promiscuous attraction of ligands within the ATP binding site of RyR2 promotes diverse gating behaviour

Abstract:

ATP is an essential constitutive regulator of cardiac ryanodine receptors (RyR2), enabling small changes in cytosolic Ca2+ to trigger large changes in channel activity. With recent landmark determinations of the full structures of RyR1 (skeletal isoform) and RyR2 using cryo-EM, and identification of the RyR1 ATP binding site, we have taken the opportunity to model the binding of fragments of ATP into RyR2 in order to investigate how the structure of the ATP site dictates the functional respon...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41598-018-33328-8

Authors


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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Oxford college:
Trinity College
Role:
Author
ORCID:
0000-0001-7777-4985
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Pharmacology
Role:
Author
More from this funder
Funding agency for:
Lindsay, C
Sitsapesan, R
Grant:
RE/08/004
RG/10/14/2857
Publisher:
Nature Publishing Group Publisher's website
Journal:
Scientific Reports Journal website
Volume:
8
Publication date:
2018-10-09
Acceptance date:
2018-09-26
DOI:
EISSN:
2045-2322
Keywords:
Pubs id:
pubs:922069
UUID:
uuid:c351b91a-b12e-4b27-aea3-37e62343d5e7
Local pid:
pubs:922069
Deposit date:
2018-09-27

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