Award details

Roles of N and C terminal domains in the domains in the activation of human eag potassium channels

Reference	C19503
Principal Investigator / Supervisor	Professor Dennis Wray
Co-Investigators / Co-Supervisors
Institution	University of Leeds
Department	Institute of Membrane & Systems Biology
Funding type	Research
Value (£)	194,000
Status	Completed
Type	Research Grant
Start date	07/10/2003
End date	06/10/2006
Duration	36 months

Abstract

Members of the ether-a-go-go family of potassium channels, eag1 and eag2, display differing activation properties. We hypothesise that these differences are due to domains in the N and C terminal regions. We aim to elucidate the molecular domains that lead to these differences in activation. For this we will make chimaeras between these two channels, express them in oocytes and study activation by two-electrode voltage-clamping. Point mutations will further clarify the key residues involved. The effects of these domains on S4 movement will also be studied by cysteine mutagenesis and gating current recordings. Proteins that bind to these domains will be identified by GST pull-down experiments and mass-spectroscopy.

Summary

unavailable

Committee	Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

I accept the terms and conditions of use (opens in new window)

export PDF file

back to list new search