The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Structural basis for Ca2+ selectivity of a voltage-gated calcium channel
Open accessAbstract
Voltage-gated calcium (CaV) channels catalyse rapid, highly selective influx of Ca2+ into cells despite a 70-fold higher extracellular concentration of Na+. How CaV channels solve this fundamental biophysical problem remains unclear. Here we report physiological and crystallographic analyses of a calcium selectivity filter constructed in the homotetrameric bacterial NaV channel NaVAb. Our results reveal interactions of hydrated Ca2+ with two high-affinity Ca2+-binding sites followed by a third lower-affinity site that would coordinate Ca2+ as it moves inward. At the selectivity filter entry, Site 1 is formed by four carboxyl side chains, which have a critical role in determining Ca2+ selectivity. Four carboxyls plus four backbone carbonyls form Site 2, which is targeted by the blocking cations Cd2+ and Mn2+, with single occupancy. The lower-affinity Site 3 is formed by four backbone carbonyls alone, which mediate exit into the central cavity. This pore architecture suggests a conduction pathway involving transitions between two main states with one or two hydrated Ca2+ ions bound in the selectivity filter and supports a ‘knock-off’ mechanism of ion permeation through a stepwise-binding process. The multi-ion selectivity filter of our CaVAb model establishes a structural framework for understanding the mechanisms of ion selectivity and conductance by vertebrate CaV channels.
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Metadata
- Authors
- Tang, L., Gamal El-Din, T. M., Payandeh, J., Martinez, G. Q., Heard, T. M., Scheuer, T., Zheng, N., & Catterall, W. A.
- Venue
- Nature
- Published
- 2013-11-24
- Volume
- 505
- Issue
- 7481
- Pages
- 56-61
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2106282816
- Cited by
- 323
- References
- 34
- FWCI
- 13.72
- Type
- journal article
- Language
- en
- Open access
- green
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