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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Aguado-Llera D,Bacarizo J,Gregorio-Teruel L,Taberner FJ,Cámara-Artigas A,Neira JL

doi

10.1016/j.febslet.2012.03.030

subject

Has Abstract

pub_date

2012-04-24 00:00:00

pages

1154-9

issue

8

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(12)00230-X

journal_volume

586

pub_type

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