The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Structural mechanism of C-type inactivation in K+ channels
Open accessAbstract
Interconversion between conductive and non-conductive forms of the K+ channel selectivity filter underlies a variety of gating events, from flicker transitions (at the microsecond timescale) to C-type inactivation (millisecond to second timescale). Here we report the crystal structure of the Streptomyces lividans K+ channel KcsA in its open-inactivated conformation and investigate the mechanism of C-type inactivation gating at the selectivity filter from channels ‘trapped’ in a series of partially open conformations. Five conformer classes were identified with openings ranging from 12 Å in closed KcsA (Cα–Cα distances at Thr 112) to 32 Å when fully open. They revealed a remarkable correlation between the degree of gate opening and the conformation and ion occupancy of the selectivity filter. We show that a gradual filter backbone reorientation leads first to a loss of the S2 ion binding site and a subsequent loss of the S3 binding site, presumably abrogating ion conduction. These structures indicate a molecular basis for C-type inactivation in K+ channels.
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Cournia, Z., Allen, T. W., Andricioaei, I., Antonny, B., Baum, D., Brannigan, G., Buchete, N.-V., Deckman, J. T., Delemotte, L., del Val, C., et al. (2015) · The Journal of Membrane Biology · doi:10.1007/s00232-015-9802-0 · Cited by 235
Molecular Mechanisms for Bacterial Potassium Homeostasis
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Metadata
- Authors
- Cuello, L. G., Jogini, V., Cortes, D. M., & Perozo, E.
- Venue
- Nature
- Published
- 2010-07
- Volume
- 466
- Issue
- 7303
- Pages
- 203-208
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2073268852
- Cited by
- 477
- References
- 49
- FWCI
- 16.90
- Type
- journal article
- Language
- en
- Open access
- green
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