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Oligomeric complexes in membrane pore formation
Reference
B13531
Principal Investigator / Supervisor
Professor Helen Saibil
Co-Investigators /
Co-Supervisors
Institution
Birkbeck College
Department
Biological Sciences
Funding type
Research
Value (£)
363,204
Status
Completed
Type
Research Grant
Start date
01/04/2001
End date
01/04/2006
Duration
60 months
Abstract
Pore-forming toxins and immune system components lyse target cells by assembling into membrane-bound, oligomeric pores. We have recently shown that it is possible to determine oligomeric pore structures in liposomes by single particle cryo-EM and 3D reconstruction. The resulting density maps, combined with atomic structure information on the soluble monomer, provide powerful tools for discerning the dramatic conformational changes that mediate the transformation of a soluble protein into a membrane-inserted pore. We plan to study the mechanism of pore formation by the bacterial toxin pneumolysin and, by the cytolytic mediator, perforin and the complement membrane attack complex in the immune response.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
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
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