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[摘要]：Transient receptor potential (TRP) proteins are sensory-related cation channels. TRPV subfamily responds to vanilloids, generating a Ca2+ current. TRPV1, a thermal-sensitive non-selective ion channel, possesses six transmembrane helices and the intracellular N- and C-terminal domains. The latter contains the PIP2 and calmodulin binding sites, the TRP domain and a temperature-responding flexible region. Although the function of C-TRPV1 is known, there are no experimental reports on its structural features. Here, we describe the conformational features of C-TRVP1, by using spectroscopic and biophysical approaches. Our results show that C-TRVP1 is an oligomeric protein, which shows features of natively unfolded proteins. Structured summary of protein interactions: C-TRPV1 and C-TRPV1 bind by dynamic light scattering (View interaction) C-TRPV1 and C-TRPV1 bind by static light scattering (View interaction) C-TRPV1 and C-TRPV1 bind by cross-linking study (View interaction) C-TRPV1 and C-TRPV1 bind by comigration in non-denaturing gel electrophoresis (View interaction) (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved. |
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