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Protein-protein interaction specificity and binding mechanism in nuclease-inhibitor complexes
Reference
B16696
Principal Investigator / Supervisor
Professor Colin Kleanthous
Co-Investigators /
Co-Supervisors
Mr Anthony Keeble
Institution
University of York
Department
Biology
Funding type
Research
Value (£)
352,568
Status
Completed
Type
Research Grant
Start date
01/07/2002
End date
30/06/2005
Duration
36 months
Abstract
Immunity (Im) proteins inactivate colicin nucleases with affinities that vary by 10 orders of magnitude but do not occlude the enzyme active site. The project will address the specificity of these complexes, focusing on the endonuclease (DNase) family of toxins, and the non-active site binding nature of Im proteins seen in RNase and DNase colicins. The proposal will address 8 areas: (1) Im protein specificity for DNases; (2) DNase specificity for Im proteins (3) Double mutant cycles; (4) Role of interfacial water and backbone hydrogen bonds; (5) Calorimetric measurements and (6) Crystallisation experiments of cognate and non-cognate complexes; (7) Probing the non-active site binding mechanism and its occurrence in other systems; (8) Defining the boundaries between the Im binding site and active site.
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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