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Characterisation of structure thermodynamics and dynamics of TPR domain interactions
Reference
B15019
Principal Investigator / Supervisor
Professor John Ladbury
Co-Investigators /
Co-Supervisors
Dr David Barford
,
Dr Mark Williams
Institution
University College London
Department
Structural Molecular Biology
Funding type
Research
Value (£)
195,584
Status
Completed
Type
Research Grant
Start date
01/11/2001
End date
01/11/2004
Duration
36 months
Abstract
TPR (tetratricopeptide repeat) motif containing proteins are important in a variety of diverse biological processes in which they mediate protein-protein interactions and the assembly of multiprotein complexes. TPR motifs are present in tandem arrays of 3-16 motifs which fold into right-handed superhelical structures. The purpose of this proposal is to understand the structural, dynamic and thermodynamic events underlying TPR-protein interactions and suggest potential routes for pharmaceutical intervention. A multi-disciplinary approach of X-ray crystallography, NMR and isothermal titration calorimetry will be applied to two biologically relevant systems, namely, Hsp90 recognition by the TPR domain of protein phosphatase 5 and recognition of perioxisomal targeting peptides by their receptor PEX5.
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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