The twisted ion-permeation pathway of a resting voltage-sensing domain

Francesco Tombola, Medha M. Pathak, Pau Gorostiza and Ehud Y. Isacoff ()
Additional contact information
Francesco Tombola: University of California
Medha M. Pathak: University of California
Pau Gorostiza: University of California
Ehud Y. Isacoff: University of California

Nature, 2007, vol. 445, issue 7127, 546-549

Abstract: Abstract Proteins containing voltage-sensing domains (VSDs) translate changes in membrane potential into changes in ion permeability or enzymatic activity1,2,3. In channels, voltage change triggers a switch in conformation of the VSD, which drives gating in a separate pore domain, or, in channels lacking a pore domain, directly gates an ion pathway within the VSD4,5. Neither mechanism is well understood6. In the Shaker potassium channel, mutation of the first arginine residue of the S4 helix to a smaller uncharged residue makes the VSD permeable to ions (‘omega current’) in the resting conformation (‘S4 down’)7. Here we perform a structure-guided perturbation analysis of the omega conductance to map its VSD permeation pathway. We find that there are four omega pores per channel, which is consistent with one conduction path per VSD. Permeating ions from the extracellular medium enter the VSD at its peripheral junction with the pore domain, and then plunge into the core of the VSD in a curved conduction pathway. Our results provide a model of the resting conformation of the VSD.

Date: 2007
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature05396 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:445:y:2007:i:7127:d:10.1038_nature05396

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature05396

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().