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Transmembrane movement of the Shaker K super(+) channel S4
We have probed internal and external accessibility of S4 residues to the membrane-impermeant thiol reagent methanethiosulfonate-ethyltrimethylammonium (MTSET) in both open and closed, cysteine-substituted Shaker K super(+) channels. Our results indicate that S4 traverses the membrane with no more th...
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| Published in: | Neuron (Cambridge, Mass.) Mass.), 1996-01, Vol.16 (2), p.387-397 |
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| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
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| container_end_page | 397 |
| container_issue | 2 |
| container_start_page | 387 |
| container_title | Neuron (Cambridge, Mass.) |
| container_volume | 16 |
| creator | Larsson, H P Baker, O S Dhillon, D S Isacoff, E Y |
| description | We have probed internal and external accessibility of S4 residues to the membrane-impermeant thiol reagent methanethiosulfonate-ethyltrimethylammonium (MTSET) in both open and closed, cysteine-substituted Shaker K super(+) 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 open. This change argues for a displacement of S4 through the plane of the membrane in which an initially intracellular residue moves to within 3 amino acids of the extracellular solution. These results demonstrate that the putative voltage-sensing charges of S4 actually reside in the membrane and that they move outward when channels open. We consider constraints placed on channel structure by these results. |
| format | article |
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| fulltext | fulltext |
| identifier | ISSN: 0896-6273 |
| ispartof | Neuron (Cambridge, Mass.), 1996-01, Vol.16 (2), p.387-397 |
| issn | 0896-6273 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15594463 |
| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS |
| title | Transmembrane movement of the Shaker K super(+) channel S4 |
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