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Drug discovery and DNA gyrase
Reference
SBD07572
Principal Investigator / Supervisor
Professor Anthony Maxwell
Co-Investigators /
Co-Supervisors
Institution
University of Leicester
Department
Biochemistry
Funding type
Research
Value (£)
139,673
Status
Completed
Type
Research Grant
Start date
01/09/1997
End date
01/09/2000
Duration
36 months
Abstract
DNA gyrase is the bacterial enzyme which supercoils DNA using the free energy of ATP hydrolysis. It is essential in bacteria as it is required for DNA replication, but it is absent from eukaryotes and therefore presents an excellent target for antibacterial agents. Our crystal determination of a second major fragment of E. coli DNA gyrase provides the basis for studying its mechanism and the atomic resolution interactions between candidate drugs. Structural analysis of the GyrA protein and the C-terminal domain of GyrB will complement previous work on the N-terminal domain of GyrB; complexes with quinolone drugs, the bacterial protein CcdB, and peptides derived from phage display will provide new leads for drug discovery.
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
Structural biology and design applications (SBD) [1996]
Funding Scheme
X – not Funded via a specific Funding Scheme
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