RNA-protein interactions are now recognised as a major control point in the regulation of gene-expression. Proteins such as HuR act to stabilise and transport specific messenger (m) RNA's, and thus determine thier translation levels. In contrast to such an important function, very little is known about these mRNA-protein interactions at an atomic level. In the current study we propose to solve the three-dimensional structures of JuR, as wel as a novel mRNA-binding domain from the Grb adapter protein family, and characterise thier interactions with their cognate mRNA sequences using X-ray cystallography and NMR spectroscopy.
|Effective start/end date||1/01/01 → 31/12/07|
- Australian Research Council (ARC): AUD67,762.00