Elongated tropomyosin, associated with actin-subunits along the surface of thin filaments, makes electrostatic interactions with clusters of conserved residues, K326, K328, and R147, on actin.
Glutamine and ATP, two of the natural ligands, were found to be extremely complementary to their binding sites, particularly in regions seen to make electrostatic interactions in the structure.
In addition, it was shown that PPAR LBD makes electrostatic interactions with DNA [42].
Residues of H4, notably Glu154, make electrostatic interactions with a second basic patch on σ2.
Lys1053 apparently makes electrostatic interactions with Asp38 in Rap and Asp1036 in plexin.
According to H3-bound G9A structure, the OH group on the side chain of H3S10 makes electrostatic interactions with the arginine 1214 of G9A.
Arg34 is another residue that approaches the channel closely enough to make electrostatic interactions, that is, with the carbonyl oxygen of Asp375.
Following initial receptor binding, the N-terminal ELR motif of CXCL8 becomes properly orientated and Glu and Arg make electrostatic interactions with the respective GPCR amino acids.
The equivalent residue in APLF, Lys36, is also in a position to make electrostatic interactions with pSer-1, although a lack of density in our structure implies that it is rather mobile.
Interestingly, the structure of G9A reveals that H3R8 is surrounded by three aspartic acids (D1074, D1078 and D1088) and that the amino groups on the side chain of H3R8 make electrostatic interactions with these three aspartic acid residues.
