title: 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.
authors.affiliation: Instituto de Biología Molecular y Celular, Universidad Miguel Hernández, 03202 Elche (Alicante), Spain.
authors.forename: David
authors.initials: D
authors.lastname: Aguado-Llera
authors.forename: Julio
authors.initials: J
authors.lastname: Bacarizo
authors.forename: Lucía
authors.initials: L
authors.lastname: Gregorio-Teruel
authors.forename: Francisco J
authors.initials: FJ
authors.lastname: Taberner
authors.forename: Ana
authors.initials: A
authors.lastname: Cámara-Artigas
authors.forename: José L
authors.initials: JL
authors.lastname: Neira
mesh_terms: D000818:Animals; D001665:Binding Sites; D055592:Biophysical Phenomena; D002147:Calmodulin / Q000378:metabolism; D002942:Circular Dichroism; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D058767:Protein Unfolding; D051381:Rats; D050916:TRPV Cation Channels / Q000737:chemistry* / Q000378:metabolism
chemical_list: D002147:Calmodulin; D050916:TRPV Cation Channels; C494484:TRPV1 receptor