All other codons of the gene remain wild-type, therefore the mutant is predicted to be non-polar.
The secondary structure of the 152 167 peptide and S158E mutant is predicted to contain a beta-strand (DNAMan software, Lynnon Biosoft).
RB1CC1 mutant was predicted to lose a microRNA-accessible loop structure at a putative binding site for the tumor-suppressive microRNA, miR-138.
The RB1CC1 3'UTR microsatellite mutant was predicted to lose a large loop structure within its putative miR-138 binding site, making disruption of the miR-138-RB1CC1 interandion and subsequent posttranscriptional downregulation likely in the mutant.
Furthermore, the MLH1 2101C>A mutant was predicted by in silico analysis to affect exon splicing ability.
Similarly, the L270M mutant is predicted to alter ligand specificity from cholesterol-binding to phospholipid-binding.
The M4 mutant is predicted to lose the shared GATA1/GATA2 site and the downstream SP1 site, The M6 mutant loses a predicted binding site for zeste homolog/TCERG1.
R70 is predicted to be involved in the interaction with IRAK-2, but different from the interaction gain with IRAK-4, the R70Q mutant is predicted to lose the IRAK-2 interaction points at position 70 of IRAK-M.
It should be noted that the Δ fur mutant is predicted to exhibit an increased iron uptake phenotype, which, in turn, might lead to increased production of hydroxyl radicals due to an excess of iron in the cytosol.
This mutant is predicted to erroneously and stochastically incorporate valine instead of alanine into growing peptide chains, nonetheless resulting in discrete defects in mediating auxin effects on cell proliferation (Perry et al., 2005).
