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Structure and molecular recognition of the KH- domain protein Vg1RBP
Reference
B11054
Principal Investigator / Supervisor
Dr Andrew Raine
Co-Investigators /
Co-Supervisors
Dr Nancy Standart
Institution
University of Cambridge
Department
Biochemistry
Funding type
Research
Value (£)
107,234
Status
Completed
Type
Research Grant
Start date
07/06/1999
End date
07/06/2001
Duration
24 months
Abstract
Vg1 RNA-binding protein (Vg1RBP) is fundamental in vegetal localisation of Vg1 mRNA in Xenopus oocytes. We have evidence that KH domains 1&2 of Vg1RBP are necessary for specific binding to the localisation element of Vg1. We propose to determine the structure of the KH1&2 didomain in complex with RNA using NMR spectroscopy. As there is currently little structural information about how KH domains in any system interact with RNA or other proteins, our results will not only lead to a better understanding of oocyte development, but also help explain the function of KH domains in other systems, including the fragile-X syndrome protein FMR1, the mouse quaking gene and genes overexpressed in pancreatic and breast cancers.
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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