[1] Initially named the RGG box, it confers a protein with the ability to bind double-stranded mRNA molecules.
The composition and structure of the arginine side chain may also allow for specific interactions with other molecules as opposed to the other positively charged amino acids, lysine and histidine.
[4] Glycine residues add flexibility to the peptide structure and promote their tendency to form intrinsically disordered regions.
The RGG motif can also drive liquid-lipid phase separation of proteins inside cells as well as in vitro.
Synthetically designed proteins containing repeating RGG motifs have been used to form droplets with tunable properties in cells and in vitro.