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https://www.um.edu.mt/library/oar/handle/123456789/29183| Title: | Contributions of the central hydrophobic residue in the PXP motif of voltage-dependent K+ channels to S6 flexibility and gating properties |
| Authors: | Imbrici, Paola Grottesi, Alessandro D'Adamo, Maria Cristina Tucker, Stephen J. Pessia, Mauro |
| Keywords: | Potassium channels Ion channels |
| Issue Date: | 2009 |
| Publisher: | Elsevier |
| Citation: | Imbrici, P., Grottesi, A., D'Adamo, M. C., Tucker, S. J., & Pessia, M. (2009). Contributions of the central hydrophobic residue in the PXP motif of voltage-dependent K+ Channels to S6 flexibility and gating properties. Biophysical Journal, 96(3), 656a. |
| Abstract: | Voltage-gated K+ channels are composed of four subunits each of which contains a voltage-sensing domain (S1-S4) and a pore domain (S5-P loop-S6). The exact molecular mechanisms underlying the opening and closing of the channel pore are still unclear, although evidence suggests that this process involves pivoting bending of the inner pore-lining S6 segments at the “helix-bundle crossing”. Shaker-like (Kv1.1) channels contain a highly conserved Pro-Val-Pro (PVP) motif at the base of S6 that produces a kink in the S6 helices and provides a flexible element thought to be essential for channel gating. |
| URI: | https://www.um.edu.mt/library/oar//handle/123456789/29183 |
| Appears in Collections: | Scholarly Works - FacM&SPB |
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|---|---|---|---|---|
| Contributions_of_the_central_hydrophobic_residue_in_the_PXP_motif_of_voltage-dependent_K+_channels_to_2009.pdf Restricted Access | 44.29 kB | Adobe PDF | View/Open Request a copy |
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