Conduction properties of the cloned Shaker K+ channel
نویسندگان
چکیده
منابع مشابه
Opening the Shaker K+ channel with hanatoxin
Voltage-activated ion channels open and close in response to changes in membrane voltage, a property that is fundamental to the roles of these channels in electrical signaling. Protein toxins from venomous organisms commonly target the S1-S4 voltage-sensing domains in these channels and modify their gating properties. Studies on the interaction of hanatoxin with the Kv2.1 channel show that this...
متن کاملStructural Implications of Fluorescence Quenching in the Shaker K+ Channel
When attached to specific sites near the S4 segment of the nonconducting (W434F) Shaker potassium channel, the fluorescent probe tetramethylrhodamine maleimide undergoes voltage-dependent changes in intensity that correlate with the movement of the voltage sensor (Mannuzzu, L.M., M.M. Moronne, and E.Y. Isacoff. 1996. Science. 271:213-216; Cha, A., and F. Bezanilla. 1997. Neuron. 19:1127-1140). ...
متن کاملTransmembrane Movement of the Shaker K+ Channel S4
We have probed internal and external accessibility of S4 residues to the membrane-impermeant thiol reagent methanethiosulfonate-ethyltrimethlammonium (MTSET) in both open and closed, cysteine-substituted Shaker K+ channels. Our results indicate that S4 traverses the membrane with no more than 5 amino acids in the closed state, and that the distribution of buried residues changes when channels o...
متن کاملProtein Rearrangements Underlying Slow Inactivation of the Shaker K+ Channel
Voltage-dependent ion channels transduce changes in the membrane electric field into protein rearrangements that gate their transmembrane ion permeation pathways. While certain molecular elements of the voltage sensor and gates have been identified, little is known about either the nature of their conformational rearrangements or about how the voltage sensor is coupled to the gates. We used vol...
متن کاملVoltage - 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...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1993
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(93)81244-x