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Structure and binding specificity of the vesicular trafficking protein SNX1

ReferenceC18024
Principal Investigator / Supervisor Professor Jon Waltho
Co-Investigators /
Co-Supervisors
Institution University of Sheffield
DepartmentMolecular Biology and Biotechnology
Funding typeResearch
Value (£) 191,928
StatusCompleted
TypeResearch Grant
Start date 01/03/2003
End date 30/11/2006
Duration45 months

Abstract

The growth signal following the activation of the EGF receptor is downregulated and switched off through a pathway of intracellular trafficking culminating in EGFR delivery to a lysosome. A key component of that trafficking is the archetypal sorting nexin, SNX1, which distinguishes the delivery target through the specific recognition of PtdIns(3,4,5)P3 using a PX domain. We will investigate the molecular basis of this specificity through the solution structure and dynamics of this unique PX domain, using heteronuclear NMR, in both the presence and absence of ligands. This will be the first structure-based study of any SNX protein (which have widespread roles in trafficking), any dimeric PX domain or any PX protein-protein interactions.

Summary

unavailable
Committee Closed Committee - Biochemistry & Cell Biology (BCB)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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