The Rev peptides that bind to the Rev-Response element are 25 residues long, and form a weak alpha helix. Of the 25 residues, there are 12 arginines, making assignment of the peptide resonances extremely difficult. In addition, the structure of the N-terminus of the peptide appears to be critical for recognition. We are examining larger fragments of Rev containing the RNA-binding domain and additional sequences toward the N-terminus. The Rev(1-50) sequence forms a compact structure in the presence of 7% trifluorethanol, and we are characterizing this structure using 15N-labeled peptide produced by overexpression. In addition, this larger protein fragment forms a specific complex with the RRE RNA. Although the spectra are of lower quality than with shorter peptides, we should be able to confirm the structure of the critical N-terminal region of the RNA-binding domain.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR000995-21
Application #
5221938
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
21
Fiscal Year
1996
Total Cost
Indirect Cost
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