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Structural studies on the regulatory cytoplasmic proteins of the NADPH oxidase

Reference	ICR07588
Principal Investigator / Supervisor	Professor Tony Segal
Co-Investigators / Co-Supervisors	Dr Benjamin Bax, Dr Frans Wientjes
Institution	University College London
Department	Medicine
Funding type	Research
Value (£)	149,651
Status	Completed
Type	Research Grant
Start date	01/10/1997
End date	01/10/2000
Duration	36 months

Abstract

The NADPH oxidase is a superoxide generating system in phagocytic leucocytes that is essential for immunity. It consists of a flavocytochrome in the membrane that is activated by three cytosolic phox proteins, p40phox, p47phox and p67phox and a small GTP binding protein p21rac. The cytosolic phox proteins can be phosphorylated and contain SH3 and proline-rich, as well as novel PX, domain. This system provides a model for examining protein/protein interactions in an activatable system. In order to better understand the interaction of these proteins and the mechanisms by which they induce electron transport through the NADPH oxidase, we propose to determine the X-ray crystal structures of complexes of the cytosolic phox proteins and the structures of individual cytosolic proteins bound to cognate (proline-rich) peptides.

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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