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Crystallographic studies of PDZ domains
Reference
ICR07595
Principal Investigator / Supervisor
Professor Peter Moody
Co-Investigators /
Co-Supervisors
Institution
University of Leicester
Department
Biochemistry
Funding type
Research
Value (£)
149,001
Status
Completed
Type
Research Grant
Start date
01/06/1997
End date
01/06/2000
Duration
36 months
Abstract
The PDZ domain is a recently discovered protein recognition module present in a variety of adaptor proteins involved or implicated in signal transduction pathways. Our crystal structure of the first such domain shows that it has a compact globular fold with a conserved hydrophobic pocket and buried arginine which form a C-terminal peptide binding site. This structure paves the way for studying other PDZ domains and their complexes with peptides. These studies will define the atomic level interactions, and together with the biochemical and modelling studies of our collaborators, will define the structural determinants of PDZ-protein recognition and specificity.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
Integration of Cellular Responses (ICR) [1996]
Funding Scheme
X – not Funded via a specific Funding Scheme
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