Here we use single-particle electron cryo- microscopy to determine the structure of full-length human TRPA1 to ∼4 Å resolution in the presence of pharmacophores, including a potent antagonist.

Julius and co-senior author Yifan Cheng, PhD, associate professor of biochemistry and biophysics, were able to capture images of TRPA1 that reveal its structure in three dimensions, including a cleft ...

For channel aficionados, this is a familiar story, so what is different about the TRPA1 structure? Paulsen and colleagues find that around 80% of TRPA1's mass is outside the channel's core ...

So the researchers decided to give it a try on TRPA1, and it worked. "The big advance here is that we can actually see the structure of the molecule — we can see the atoms in the molecule ...

The findings from this study were published recently in Nature through an article entitled “Structure of the TRPA1 ion channel suggests regulatory mechanisms.” Using a technique called ...

Julius and co-senior author Yifan Cheng, Ph.D., associate professor of biochemistry and biophysics, were able to capture images of TRPA1 that reveal its structure in three dimensions, including a ...

Though scientific knowledge of TRPA1’s roles in detecting sensations, both positive and negative, has been developing for at least a decade now, the April 2015 discovery of its structure represents a ...

But TRPA1 manages to recognize many differently shaped irritant ... “The days of just getting one structure and publishing a paper are over. Now we have the technology to tell complex, interesting ...

Transient Receptor Potential Ankyrin 1 (TRPA1) is a non-selective cation channel that is expressed in a subset of nociceptive afferent sensory nerves. When activated, TRPA1 can evoke nociceptive ...

Proposed model for how acetic acid might activate the ion channel TRPA1. A new study in the Journal of General Physiology identifies TRPA1 as the sensor in animals responsible for identifying weak ...