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 Lettjournal_title
FEBS lettersauthors
Aguado-Llera D,Bacarizo J,Gregorio-Teruel L,Taberner FJ,Cámara-Artigas A,Neira JLdoi
10.1016/j.febslet.2012.03.030subject
Has Abstractpub_date
2012-04-24 00:00:00pages
1154-9issue
8eissn
0014-5793issn
1873-3468pii
S0014-5793(12)00230-Xjournal_volume
586pub_type
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