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Addenda
Insights into the Roles of Conserved and Divergent Residues in the Ankyrin Repeats of TRPV Ion Channels
Christopher B. Phelps, Erik Procko, Polina V. Lishko, Ruqui R. Wang and Rachelle Gaudet
volume 1 | issue 3
May/June 2007Pages: 148 - 151
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Ion channels are often modulated by intracellular calcium levels. TRPV1, a channel responsible for the burning pain sensation in response to heat, acid or capsaicin, is desensitized at high intracellular calcium concentrations. We recently identified a multiligand-binding site in the N-terminal ankyrin repeat domain (ARD) of TRPV1 that binds ATP and sensitizes the channel. Calcium-calmodulin binds the same site and is necessary for calcium-mediated TRPV1 desensitization. Here, we examine in more detail the conservation of this TRPV1 multiligand-binding site in other species. Furthermore, using sequence analysis, we determine that the unusually twisted shape of the TRPV1-ARD is likely conserved in other TRPV channels, but not in the ARDs of other TRP subfamilies.
Authors
Christopher B. Phelps
Harvard University, Cambridge, MA
Erik Procko
Harvard University, Cambridge, MA
Polina V. Lishko
Harvard University, Cambridge, MA
Ruqui R. Wang
Harvard University, Cambridge, MA
Rachelle Gaudet
Harvard University, Cambridge, MA
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.