Figure 1 | Scientific Reports

Figure 1

From: Phosphorylation of the Transient Receptor Potential Ankyrin 1 by Cyclin-dependent Kinase 5 affects Chemo-nociception

Figure 1

Protein model of TRPA1 ankyrin repeat domains with putative phosphorylation sites. TRPA1 is a large homotetrameric pore-forming channel. (A) cryo-EM was used to solve the structure of ankyrin repeat (AR) domains from AR12 all the way through the 6 transmembrane domains. (B) One member of the homotetrameric complex is shown including the locations of all 6 putative Cdk5 phosphorylation sites (pink) and the EF hand domain (green). ARs 1–11 (light blue) were modeled separately. (C) At Thr485, an empty pocket can be observed adjacent to the EF hand. Structural modeling (D,E) suggests this binding pocket is approximately the size of a phospho-threonine (pThr) residue, suggesting that the side chain of this Thr residue, once phosphorylated, would fill the pocket.

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