The helical character of the S6 segment of TRPV1 channels.
The era of molecular structure of ion channels has revealed that their transmembrane segments are alpha helices, as was suspected from hydropathy analysis and experimental data. TRP channels are recent additions to the known families of ion channels, and little structural data is available. In a recent work, we explored the conformational changes occurring at the putative S6 segment of TRPV1 channels; and we observed a periodicity of chemical modification of residues suggestive of an alpha helical structure. Further analysis of the periodicity of the disposition of hydrophobic residues in the S6 segment, suggests that the general architecture of the TRPV1 S6 segment, is very similar to that of voltage-dependent channels of known structure--an aqueous cavity lined by an amphipathic alpha helix, with most of the hydrophobic residues pointing into it.
Islas
León D
LD
Departamento de Fisiología, Universidad Nacional Autónoma de México, México D.F., México.
Salazar
Héctor
H
Jara-Oseguera
Andrés
A
Nieto-Posadas
Andrés
A
Llorente
Itzel
I
Rangel-Yescas
Gisela
G
Rosenbaum
Tamara
T
D000818:Animals; D001703:Biophysics / Q000379:methods; D020285:Cryoelectron Microscopy / Q000379:methods; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007473:Ion Channels / Q000737:chemistry; D007477:Ions; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D050916:TRPV Cation Channels / Q000737:chemistry*
D007473:Ion Channels; D007477:Ions; D050916:TRPV Cation Channels; C494484:TRPV1 receptor