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Structural determination of full-length myristoylated HIV-1 Nef complexed with Fyn SH3 domain by X-ray crystallography
Reference
B19796
Principal Investigator / Supervisor
Dr Joachim Jaeger
Co-Investigators /
Co-Supervisors
Dr Caitriona Dennis
,
Dr MPG Harris
Institution
University of Leeds
Department
Inst of Molecular & Cellular Biology
Funding type
Research
Value (£)
73,394
Status
Completed
Type
Research Grant
Start date
15/11/2003
End date
14/11/2004
Duration
12 months
Abstract
HIV-1 Nef is expressed in abundance during early stages of viral replication and is thought to be a major determinant in disease progression from viral infection to the acquired immunodeficiency syndrome (AIDS). The protein is targeted and anchored to the cellular membrane via a myristoylated N-terminal glycine residue where it carried out a number of functions such as down-regulation of CD4 and the perturbation of T-cell signalling through direct binding of Src homology domains. The three-dimensional structure of full-length myristoylated Nef is as yet unknown. Using X-ray crystallography, we will determine this structure alone and, using an existing orthorhombic crystal form, in complex with Fyn and other cellular targets.
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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