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| Content Provider | Springer Nature Link |
|---|---|
| Author | Pérez Cornejo, Patricia |
| Copyright Year | 1999 |
| Abstract | The participation of an extracellular loop in C-type inactivation of voltage-gated K+ channels was investigated. A wild-type phenylalanine (at position 425) between the fifth putative transmembrane segment (S5) and the pore region of the Shaker K+ channel was mutated to a histidine and the functional consequences of protonating the imidizole group of the histidine were examined. C-type inactivation of both wild-type and mutant channels was sensitive to external pH over the range of 5.2–8. The pH dependence of wild-type channels was characterized by an apparent pK value of 5.0. The inactivation kinetics of F425H mutant channels had a pH dependence with a pK of 5.8 – in addition to the pH dependence of the wild-type channels. Moreover, at pH 7 and 8 the voltage dependence of C-type inactivation kinetics was manifest only in the F425H mutant channels. C-type inactivation in wild-type channels involves a chemical group with a low pK. Taken together, these results suggest that residues located in the extracellular S5-pore loop of the Shaker K+ channel participate in C-type inactivation. |
| Starting Page | 865 |
| Ending Page | 870 |
| Page Count | 6 |
| File Format | |
| ISSN | 00316768 |
| Journal | Pflügers Archiv |
| Volume Number | 437 |
| Issue Number | 6 |
| e-ISSN | 14322013 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 1999-04-22 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology Physiology (medical) Clinical Biochemistry |
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