دورية أكاديمية
Kv channel gating requires a compatible S4-S5 linker and bottom part of S6, constrained by non-interacting residues.
| العنوان: | Kv channel gating requires a compatible S4-S5 linker and bottom part of S6, constrained by non-interacting residues. |
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| المؤلفون: | Labro AJ; Laboratory for Molecular Biophysics, Physiology, and Pharmacology, Department of Biomedical Sciences, University of Antwerp, 2610 Antwerp, Belgium., Raes AL, Grottesi A, Van Hoorick D, Sansom MS, Snyders DJ |
| المصدر: | The Journal of general physiology [J Gen Physiol] 2008 Dec; Vol. 132 (6), pp. 667-80. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Rockefeller University Press Country of Publication: United States NLM ID: 2985110R Publication Model: Print Cited Medium: Internet ISSN: 1540-7748 (Electronic) Linking ISSN: 00221295 NLM ISO Abbreviation: J Gen Physiol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: New York, N.Y. : Rockefeller University Press Original Publication: New York, N.Y. : Rockefeller Institute for Medical Research, c1918- |
| مواضيع طبية MeSH: | Ion Channel Gating*/genetics, Energy Transfer/*physiology , Potassium Channels, Voltage-Gated/*metabolism , Protein Interaction Domains and Motifs/*physiology, Amino Acid Sequence ; Amino Acid Substitution ; Humans ; Kinetics ; Membrane Potentials ; Mutagenesis, Site-Directed ; Potassium Channels, Voltage-Gated/chemistry ; Potassium Channels, Voltage-Gated/genetics ; Protein Structure, Secondary/physiology ; Structure-Activity Relationship |
| مستخلص: | Voltage-dependent K(+) channels transfer the voltage sensor movement into gate opening or closure through an electromechanical coupling. To test functionally whether an interaction between the S4-S5 linker (L45) and the cytoplasmic end of S6 (S6(T)) constitutes this coupling, the L45 in hKv1.5 was replaced by corresponding hKv2.1 sequence. This exchange was not tolerated but could be rescued by also swapping S6(T). Exchanging both L45 and S6(T) transferred hKv2.1 kinetics to an hKv1.5 background while preserving the voltage dependence. A one-by-one residue substitution scan of L45 and S6(T) in hKv1.5 further shows that S6(T) needs to be alpha-helical and forms a "crevice" in which residues I422 and T426 of L45 reside. These residues transfer the mechanical energy onto the S6(T) crevice, whereas other residues in S6(T) and L45 that are not involved in the interaction maintain the correct structure of the coupling. |
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| المشرفين على المادة: | 0 (Potassium Channels, Voltage-Gated) |
| تواريخ الأحداث: | Date Created: 20081126 Date Completed: 20090210 Latest Revision: 20220309 |
| رمز التحديث: | 20240628 |
| مُعرف محوري في PubMed: | PMC2585865 |
| DOI: | 10.1085/jgp.200810048 |
| PMID: | 19029374 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1540-7748 |
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| DOI: | 10.1085/jgp.200810048 |