Structural motifs underlying voltage-dependent K+ channel function
نویسندگان
چکیده
منابع مشابه
Voltage - dependent Structural Interactions in the Shaker K 1 Channel
Using a strategy related to intragenic suppression, we previously obtained evidence for structural interactions in the voltage sensor of Shaker K 1 channels between residues E283 in S2 and R368 and R371 in S4 (Tiwari-Woodruff, S.K., C.T. Schulteis, A.F. Mock, and D.M. Papazian. 1997. Biophys . J . 72:1489–1500). Because R368 and R371 are involved in the conformational changes that accompany vol...
متن کاملVoltage-Dependent Structural Interactions in the Shaker K+ Channel
Using a strategy related to intragenic suppression, we previously obtained evidence for structural interactions in the voltage sensor of Shaker K(+) channels between residues E283 in S2 and R368 and R371 in S4 (Tiwari-Woodruff, S.K., C.T. Schulteis, A.F. Mock, and D. M. Papazian. 1997. Biophys. J. 72:1489-1500). Because R368 and R371 are involved in the conformational changes that accompany vol...
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The intramembrane molecular events underlying activation gating in the Streptomyces K+ channel were investigated by site-directed spin-labeling methods and electron paramagnetic resonance spectroscopy. A comparison of the closed and open conformations of the channel revealed periodic changes in spin-label mobility and intersubunit spin-spin interaction consistent with rigid-body movements of th...
متن کاملStructural basis for the inhibition of voltage-dependent K+ channel by gating modifier toxin
Voltage-dependent K(+) (Kv) channels play crucial roles in nerve and muscle action potentials. Voltage-sensing domains (VSDs) of Kv channels sense changes in the transmembrane potential, regulating the K(+)-permeability across the membrane. Gating modifier toxins, which have been used for the functional analyses of Kv channels, inhibit Kv channels by binding to VSD. However, the structural basi...
متن کاملVoltage - dependent Structural Interactions in the Shaker K 1 Channel Seema
Using a strategy related to intragenic suppression, we previously obtained evidence for structural interactions in the voltage sensor of Shaker K 1 channels between residues E283 in S2 and R368 and R371 in S4 (Tiwari-Woodruff, S.K., C.T. Schulteis, A.F. Mock, and D.M. Papazian. 1997. Biophys . J . 72:1489–1500). Because R368 and R371 are involved in the conformational changes that accompany vol...
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ژورنال
عنوان ژورنال: Kidney International
سال: 1995
ISSN: 0085-2538
DOI: 10.1038/ki.1995.372