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The structural and functional role of co-and post- translational modifications at the N-terminus of the HIV-1 Nef protein

Reference	C12902
Principal Investigator / Supervisor	Dr MPG Harris
Co-Investigators / Co-Supervisors	Dr Joachim Jaeger
Institution	University of Leeds
Department	Inst of Molecular & Cellular Biology
Funding type	Research
Value (£)	149,632
Status	Completed
Type	Research Grant
Start date	05/06/2000
End date	05/06/2003
Duration	36 months

Abstract

The Nef protein of HIV-1 is a myristoylated phosphoprotein that has been shown to be critical for viral pathogenesis. Myristoylation has been shown to be important for Nef function but its role in the structure of the native protein has not been addressed. Full length myristoylated Nef protein will be produced using baculovirus or E. coli expression systems and subjected to structural analysis. Evidence from our laboratory and others points to the N- terminus as a site of phosphorylation; we will define the sites of phosphorylation and determine whether phosphorylation modulates the interactions of Nef with cellular membranes. Lastly the biochemical nature of the interactions between Nef and cellular membranes will be investigated.

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	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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