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Crystallographic analysis of ligand binding to human serum albumin (HSA)
Reference
B12706
Principal Investigator / Supervisor
Professor Stephen Curry
Co-Investigators /
Co-Supervisors
Institution
Imperial College London
Department
Biological Sciences
Funding type
Research
Value (£)
181,328
Status
Completed
Type
Research Grant
Start date
20/03/2000
End date
17/07/2003
Duration
40 months
Abstract
Human serum albumin (HSA) is an important plasma protein that binds fatty acids, a wide range of drugs and surface proteins of certain pathogenic bacteria. The interactions of HSA with its various ligands have been studied for many years, but there remains a dearth of structural information. Recently we published the first structure of HSA bound to fatty acid, its primary ligand. We now wish to extend our crystallographic structural analysis of HSA to incorporate (1) additional fatty acids (both saturated and unsaturated); (2) a range of drug compounds known to bind to the two primary drug binding sites on the protein (3) the GA- type albumin binding domain from bacterial surface proteins. This study should provide a wealth of new information on structural aspects of ligand binding to HSA.
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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