Referenced in: none

Automatically associated channels: TRP , TRPV , TRPV1

Title: Biophysical characterization of the isolated C-terminal region of the transient receptor potential vanilloid 1.

Authors: David Aguado-Llera, Julio Bacarizo, Lucía Gregorio-Teruel, Francisco J Taberner, Ana Cámara-Artigas, José L Neira

Journal, date & volume: FEBS Lett., 2012 Apr 24 , 586, 1154-9

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/22575650

Abstract
Transient receptor potential (TRP) proteins are sensory-related cation channels. TRPV subfamily responds to vanilloids, generating a Ca(2+) 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 PIP(2) 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.