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Structural determinants of integrin adhesiveness
Reference
B06828
Principal Investigator / Supervisor
Dr Robert Liddington
Co-Investigators /
Co-Supervisors
Institution
University of Leicester
Department
Biochemistry
Funding type
Research
Value (£)
45,180
Status
Completed
Type
Research Grant
Start date
01/11/1996
End date
01/11/1997
Duration
12 months
Abstract
Integrin-mediated cell adhesion is required for development, tumour metastasis, haemostasis and the inflammation response. Our crystallographic studies of the integrin l-domain have led to hypotheses concerning integrin-ligand interactions and the pathway of integrin activation. We propose to test and extend these hypotheses by determining atomic resolution crystal structures of (1) the complex between the LFA-l domain and suitable fragments of the natural counter-receptor, ICAM; (2) the major ligand binding domain of the beta-chain; and (3) a related l-domain from integrin alpha2beta1. These studies should lead to new insights into the molecular basis of cell adhesion, and provide improved therapeutic strategies in pathological states.
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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