Insights into the roles of conserved and divergent residues in the ankyrin repeats of TRPV ion channels |
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Authors: | Phelps Christopher B Procko Erik Lishko Polina V Wang Ruiqi R Gaudet Rachelle |
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Affiliation: | Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02318, USA. |
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Abstract: | 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. |
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