Award details

Characterisation of structure thermodynamics and dynamics of TPR domain interactions

ReferenceB15019
Principal Investigator / Supervisor Professor John Ladbury
Co-Investigators /
Co-Supervisors
Dr David Barford, Dr Mark Williams
Institution University College London
DepartmentStructural Molecular Biology
Funding typeResearch
Value (£) 195,584
StatusCompleted
TypeResearch Grant
Start date 01/11/2001
End date 01/11/2004
Duration36 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 TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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