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The 3-D structure of Trunk a putative cystine-knot ligand and its interactions with the receptor Tor
Reference
9708957
Principal Investigator / Supervisor
Professor Sir Tom Blundell
Co-Investigators /
Co-Supervisors
Institution
University of Cambridge
Department
Biochemistry
Funding type
Research
Value (£)
108,080
Status
Completed
Type
Research Grant
Start date
01/10/1997
End date
01/10/1999
Duration
24 months
Abstract
Our objective is to test the hypothesis that the cystine-knot fold occurs in Trunk, a recently defined ligand for the Tor receptor. The cystine-knot fold was first described in NGF and subsequently in other growth factors and glycoprotein hormones. It has recently been identified in coagulogen of the blood clotting pathway in Limulus and predicted for Spatzle, a factor involved in the development of the poles of the Drosophila embryo. Like NGF, coagulogen and Spatzle, Trunk is regulated by proteolysis, but evidence from the sequence pattern for a cystine knot is far more speculative. We aim to express, purify, crystallise and determine the three-dimensional structure by X-ray analysis of Trunk in order to test this hypothesis, and to carry out preliminary studies on its interactions with the Tor receptor.
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
ROPA 1997 (ROPA1997) [1997]
Funding Scheme
X – not Funded via a specific Funding Scheme
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