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Determination of the three dimensional solution structure of human CD5 domain 1
Reference
B07027
Principal Investigator / Supervisor
Dr Paul Driscoll
Co-Investigators /
Co-Supervisors
Institution
University College London
Department
Structural Molecular Biology
Funding type
Research
Value (£)
186,616
Status
Completed
Type
Research Grant
Start date
25/10/1996
End date
25/10/1999
Duration
36 months
Abstract
The aim of the project is to determine the three-dimensional structure of the N-terminal domain of the T- and B-cell surface antigen CD5. This domain is a member of the so-called cysteine-rich scavenger receptor superfamily, for which no structure has been previously determined. We have preliminary data to show that the protein can be expressed in good yield in mammalian and yeast cell culture. We will develop expression of CD5 domain 1 in a Pichia pastoris yeast secretion system. Then we will apply the battery of modern day triple resonance NMR techniques to solve the three dimensional solution structure of the domain. Knowledge of the structure will lead to structure/function studies for CD5 and the potential to model other members of the scavenger receptor cysteine rich superfamily of domains.
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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