Structure of the PR domain of RIZ1 tumor suppressor
EMSL Project ID
7391
Abstract
RIZ1 is a PR domain containing histone lysine methyltransferase with tumor suppressor activity that provides a link between dietary and genetic causes of cancer. We plan to determine the structure of the PR domain from RIZ1, using standard double and triple resonance NMR experiments. However, since we can work only at submillimolar protein concentrations with RIZ1, the NOESY experiments will greatly benefit from data acquisition at high field to improve resolution and sensitivity. We have been awarded two weeks of 750 MHz time at PNNL in the current cycle to acquire 4D NOESY data sets. We estimate that we need an additional three weeks of 750 MHz spectrometer time to complete acquisition of the 4D NOESY spectra. Such experiments proved to be very helpful in resolving ambiguities during our previous structure determination projects.Project Details
Project type
Capability Research
Start Date
2004-05-01
End Date
2005-05-16
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
Briknarova, K., Zhou, X., Satterthwait, A., Hoyt, D.W., Ely, K.R., and Huang, S. 2008. "Structural studies of the SET domain from RIZ1 tumor suppressor." Biochemical and Biophysical Research Communications, 366: 807-813.