Three molecules of the cholesterol drug atorvastatin can sit together in a single pocket of a calcium channel in muscle cells and force it open, according to a cryo-electron microscopy study from the University of British Columbia. A channel stuck open lets calcium leak continuously into muscle cells, which can injure the tissue. The team proposes that this is a route to the muscle pain, weakness and fatigue that lead some people to stop taking statins.
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The picture is of one drug on one protein. The researchers studied atorvastatin only, and they describe the wider relevance as a suggestion: the findings point to an effect that may be common across the drug class, but no other statin was shown to behave the same way. The work is structural, built from cryo-electron microscopy images of the protein, and the sources describe no clinical testing, patient samples or measurement of calcium leak in living muscle.
The Ryanodine Receptor RyR1 and Three Statin Molecules
The paper, “Cryo-electron microscopy reveals sequential binding and activation of Ryanodine Receptors by statin triplets”, appeared in Nature Communications in November 2025. Its authors are Steven Molinarolo, Carmen R. Valdivia, Héctor H. Valdivia and Filip Van Petegem. Molinarolo, a postdoctoral researcher in UBC’s Department of Biochemistry and Molecular Biology, is the lead author, and Van Petegem, a professor at UBC’s Life Sciences Institute, is the senior author, with collaborators at the University of Wisconsin-Madison. ScienceDaily’s repost is dated Oct. 20, 2026, nearly a year after the journal paper, so the finding itself dates to late 2025.
The protein is the ryanodine receptor 1, or RyR1, which regulates the release of calcium that muscle cells use to contract and normally opens only when a muscle needs to work. According to UBC’s release, the first statin molecule binds while the channel is closed and primes it to open, and two more then wedge into the pocket and push it fully open. The atomic model was built by single-particle cryo-electron microscopy, and the database entry for the atorvastatin-bound open structure lists a resolution of 3.37 angstroms and a rabbit RyR1, deposited in May 2025.
Molinarolo said the team could see, almost atom by atom, how statins latch onto the channel. Van Petegem called it the first time there had been a clear picture of how statins activate it. Those are statements about structure. The link to symptoms in patients is the paper’s proposal, resting on the reported ability of continuous calcium leakage to damage muscle tissue, and the coordinates were released publicly in January 2026, so other groups can examine the model themselves.
Cryo-electron microscopy works by freezing protein samples and imaging them in many orientations, then averaging the images into a three-dimensional model, which is how the team could place individual atorvastatin molecules inside the pocket. The database entry for the open-channel structure was released on Jan. 28, 2026, and cites the Nature Communications paper, article number 11508.
How Common Statin Muscle Symptoms Are
Statins are taken by more than 200 million people worldwide, and the Life Sciences Institute’s account says severe muscle damage affects only a small fraction of them. Milder aches and fatigue are far more common, though none of the sources quantifies them, and those symptoms can push patients to stop treatment. The structural result does not say why one patient is affected and another is not, a question the images cannot answer on their own.
That gap matters for any claim of explaining muscle pain. A binding site that every statin user’s muscle carries cannot by itself account for why only some develop symptoms, and the sources describe no test of what separates affected patients from unaffected ones. UBC’s release also frames class-wide relevance as a suggestion, noting only that the findings suggest the effect may be common across the drug class.
What Safer Statins Would Require
The practical hope is drug design. Van Petegem said the structure gives a roadmap for designing statins that do not interact with muscle tissue, and the UBC release says the aim is to alter the parts of the molecule responsible for side effects while keeping the cholesterol-lowering activity. The authors say the findings could pave the way for safer statins and could help prevent symptoms, but additional research and drug development will be needed.
No redesigned statin has been tested, so there is nothing yet for patients to act on, and the sources do not describe any change to prescribing. The funding for the work is not stated in the release or in ScienceDaily’s repost. What the structure supplies is a defined pocket and a defined sequence of three binding events, which gives chemists something specific to design around. Van Petegem said the goal is to make statins even safer so that patients can benefit without fear of serious side effects. Whether other statins use the same pocket, and whether a modified molecule keeps its cholesterol-lowering action, remain open questions that this study does not answer.
This article was produced with the assistance of AI and reviewed by Morning Overview editors prior to publication.
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