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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hu, Hongzhen Chen, Zongyun Yang, Weishan Xiang, Fang Feng, Jing Cao, Zhijian Li, Wenxin Wu, Yingliang Xie, Zili |
| Description | Author Affiliation: Feng J ( From the State Key Laboratory of Virology, College of Life Sciences and.); Yang W ( From the State Key Laboratory of Virology, College of Life Sciences and.); Xie Z ( From the State Key Laboratory of Virology, College of Life Sciences and.); Xiang F ( From the State Key Laboratory of Virology, College of Life Sciences and.); Cao Z ( From the State Key Laboratory of Virology, College of Life Sciences and the Center for BioDrug Research, Wuhan University, Wuhan 430072, China and.); Li W ( From the State Key Laboratory of Virology, College of Life Sciences and the Center for BioDrug Research, Wuhan University, Wuhan 430072, China and.); Hu H ( the Center for the Study of Itch, Washington University Pain Center, Department of Anesthesiology, Washington University School of Medicine, St. Louis, Missouri 63110.); Chen Z ( From the State Key Laboratory of Virology, College of Life Sciences and chenzy2005@126.com.); Wu Y ( From the State Key Laboratory of Virology, College of Life Sciences and the Center for BioDrug Research, Wuhan University, Wuhan 430072, China and ylwu@whu.edu.cn.) |
| Abstract | Among the three extracellular domains of the tetrameric voltage-gated K(+) (Kv) channels consisting of six membrane-spanning helical segments named S1-S6, the functional role of the S1-S2 linker still remains unclear because of the lack of a peptide ligand. In this study, the Kv1.3 channel S1-S2 linker was reported as a novel receptor site for human ß-defensin 2 (hBD2). hBD2 shifts the conductance-voltage relationship curve of the human Kv1.3 channel in a positive direction by nearly 10.5 mV and increases the activation time constant for the channel. Unlike classical gating modifiers of toxin peptides from animal venoms, which generally bind to the Kv channel S3-S4 linker, hBD2 only targets residues in both the N and C termini of the S1-S2 linker to influence channel gating and inhibit channel currents. The increment and decrement of the basic residue number in a positively charged S4 sensor of Kv1.3 channel yields conductance-voltage relationship curves in the positive direction by â ¼31.2 mV and 2-4 mV, which suggests that positively charged hBD2 is anchored in the channel S1-S2 linker and is modulating channel activation through electrostatic repulsion with an adjacent S4 helix. Together, these findings reveal a novel peptide ligand that binds with the Kv channel S1-S2 linker to modulate channel activation. These findings also highlight the functional importance of the Kv channel S1-S2 linker in ligand recognition and modification of channel activation. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 25 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-06-19 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Ion Channel Gating Physiology Kv1.3 Potassium Channel Metabolism Membrane Potentials Beta-Defensins Binding Sites HEK293 Cells Chemistry Genetics Protein Binding Protein Structure, Secondary Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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