| Value |
500
Fold
|
| Organism |
HIV |
| Reference |
Daugherty MD, D'Orso I, Frankel AD. A solution to limited genomic capacity: using adaptable binding surfaces to assemble the functional HIV Rev oligomer on RNA. Mol Cell. 2008 Sep 2631(6):pp. 825-826PubMed ID18922466
|
| Method |
Proteins were expressed in e. coli. Full-length Rev was purified by Ni-NTA affinity chromatography and cleaved by TEV using standard procedures. RNA-Binding Gel Shift Assays. NMR, RNA Export Reporter Assays. |
| Comments |
Previous studies have shown that affinity of Rev monomers remains approximately constant at 20–100 nM. This study showed affinity to oligomeric complex (KD)~100pM. The 116 amino acid HIV-1 Rev protein binds to the 350 nt Rev response element (RRE) RNA found in the introns of partially spliced and unspliced viral mRNAs, forming a large RNP that directs their transport to the cytoplasm before splicing is completed. |
| Entered by |
Uri M |
| ID |
102606 |