The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
Molecular basis for pore blockade of human Na + channel Na v 1.2 by the μ-conotoxin KIIIA
Abstract
Targeting sodium channels: Voltage-gated sodium (Na v ) channels have been implicated in cardiac and neurological disorders. There are many subtypes of these channels, making it challenging to develop specific therapeutics. A core α subunit is sufficient for voltage sensing and ion conductance, but function is modulated by β subunits and by natural toxins that can either act as pore blockers or gating modifiers (see the Perspective by Chowdhury and Chanda). Shen et al. present the structures of Na v 1.7 in complex with both β1 and β2 subunits and with animal toxins. Pan et al. present the structure of Na v 1.2 bound to β2 and a toxic peptide, the µ-conotoxin KIIIA. The structure shows why KIIIA is specific for Na v 1.2. These and other recently determined Na v structures provide a framework for targeted drug development. Science , this issue p. 1303 , p. 1309 ; see also p. 1278
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Metadata
- Authors
- Pan, X., Li, Z., Huang, X., Huang, G., Gao, S., Shen, H., Liu, L., Lei, J., & Yan, N.
- Venue
- Science
- Published
- 2019-03-22
- Volume
- 363
- Issue
- 6433
- Pages
- 1309-1313
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2911919235
- Cited by
- 257
- References
- 49
- FWCI
- 10.74
- Type
- journal article
- Language
- en
- Open access
- closed
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