by Joel Mackay | Dec 4, 2020 | Structure Gallery |
[ PDB file ] [ PubMed link ] This CHANCE peptide was one of two (+DFF5) designed to mimic the GATA-binding surface of the transcriptional repressor U-shaped. NMR structural work showed both that DFF7 was well-folded (right) and that the grafted residues occupied...
by Joel Mackay | Dec 4, 2020 | Structure Gallery |
[ PDB file ] [ PubMed link ] This CHANCE peptide was designed to mimic the GATA-binding surface of the transcriptional repressor U-shaped. We have previously defined the surface involved in this interaction, and we attempted to transplant this surface onto the minimal...
by Joel Mackay | Dec 4, 2020 | Structure Gallery |
[ PDB file ] [ PubMed link ] This is one of the first CHANCE peptides that was designed to emulate the binding function of another protein. The N-terminal nucleocapsid domain (NUC1, left) of the HIV-1 nucleocapsid protein is able to bind to a short oligonucleotide...
by Joel Mackay | Dec 4, 2020 | Structure Gallery |
[ PDB file ] [ PubMed link ] This is a second minimalised version of the CHANCE domain. This time, 13 of the 25 residues have been mutated (mostly to alanine), and the fold is retained. These two stripped down domains retain only the zinc-binding residues and the...
by Joel Mackay | Dec 4, 2020 | Structure Gallery |
[ PDB file ] [ PubMed link ] This is a minimalised version of the CHANCE domain. 12 of the 25 residues have been mutated (mostly to alanine), but the fold is retained. This ‘stripping down’ of the surface of the domain is the first step in re-designing the...