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- Publisher Website: 10.1038/s41586-018-0134-y
- Scopus: eid_2-s2.0-85048498326
- PMID: 29769723
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Article: Structure of a volume-regulated anion channel of the LRRC8 family
Title | Structure of a volume-regulated anion channel of the LRRC8 family |
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Authors | |
Issue Date | 2018 |
Citation | Nature, 2018, v. 558, n. 7709, p. 254-259 How to Cite? |
Abstract | Volume-regulated anion channels are activated in response to hypotonic stress. These channels are composed of closely related paralogues of the leucine-rich repeat-containing protein 8 (LRRC8) family that co-assemble to form hexameric complexes. Here, using cryo-electron microscopy and X-ray crystallography, we determine the structure of a homomeric channel of the obligatory subunit LRRC8A. This protein conducts ions and has properties in common with endogenous heteromeric channels. Its modular structure consists of a transmembrane pore domain followed by a cytoplasmic leucine-rich repeat domain. The transmembrane domain, which is structurally related to connexin proteins, is wide towards the cytoplasm but constricted on the outside by a structural unit that acts as a selectivity filter. An excess of basic residues in the filter and throughout the pore attracts anions by electrostatic interaction. Our work reveals the previously unknown architecture of volume-regulated anion channels and their mechanism of selective anion conduction. |
Persistent Identifier | http://hdl.handle.net/10722/343263 |
ISSN | 2023 Impact Factor: 50.5 2023 SCImago Journal Rankings: 18.509 |
DC Field | Value | Language |
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dc.contributor.author | Deneka, Dawid | - |
dc.contributor.author | Sawicka, Marta | - |
dc.contributor.author | Lam, Andy K.M. | - |
dc.contributor.author | Paulino, Cristina | - |
dc.contributor.author | Dutzler, Raimund | - |
dc.date.accessioned | 2024-05-10T09:06:45Z | - |
dc.date.available | 2024-05-10T09:06:45Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | Nature, 2018, v. 558, n. 7709, p. 254-259 | - |
dc.identifier.issn | 0028-0836 | - |
dc.identifier.uri | http://hdl.handle.net/10722/343263 | - |
dc.description.abstract | Volume-regulated anion channels are activated in response to hypotonic stress. These channels are composed of closely related paralogues of the leucine-rich repeat-containing protein 8 (LRRC8) family that co-assemble to form hexameric complexes. Here, using cryo-electron microscopy and X-ray crystallography, we determine the structure of a homomeric channel of the obligatory subunit LRRC8A. This protein conducts ions and has properties in common with endogenous heteromeric channels. Its modular structure consists of a transmembrane pore domain followed by a cytoplasmic leucine-rich repeat domain. The transmembrane domain, which is structurally related to connexin proteins, is wide towards the cytoplasm but constricted on the outside by a structural unit that acts as a selectivity filter. An excess of basic residues in the filter and throughout the pore attracts anions by electrostatic interaction. Our work reveals the previously unknown architecture of volume-regulated anion channels and their mechanism of selective anion conduction. | - |
dc.language | eng | - |
dc.relation.ispartof | Nature | - |
dc.title | Structure of a volume-regulated anion channel of the LRRC8 family | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1038/s41586-018-0134-y | - |
dc.identifier.pmid | 29769723 | - |
dc.identifier.scopus | eid_2-s2.0-85048498326 | - |
dc.identifier.volume | 558 | - |
dc.identifier.issue | 7709 | - |
dc.identifier.spage | 254 | - |
dc.identifier.epage | 259 | - |
dc.identifier.eissn | 1476-4687 | - |