Interactions between the conserved acidic and associated residues in the L16 3/10 Helix.

<p>Residue coloring scheme is similar to <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0119636#pone.0119636.g003" target="_blank">Fig. 3</a> (i.e. cyan sticks representation denotes MAPK specific residues and light orange/tan sticks denotes subfamily (e.g. JNK) specific residues). A) Interactions of the MAPK specific salt bridge in the apo, unphosphorylated p38α (PDBID: 1P38). B) Interactions of the corresponding region in phosphorylated, apo form of p38α (PDBID: 3PY3). C) Interactions of the salt bridge in ATP analog bound, dually phosphorylated state in p38γ (PDBID: 1CM8). D) Interactions in apo, unphosphorylated ERK5 (PDBID: 4IC8). E) Interactions in ATP analogue bound, unphosphorylated ERK5 (PDBID: 4IC7). F) Interactions in phosphorylated, ATP bound ERK2 (PDBID: 2ERK). G) Disengagement of canonical salt bridge in apo ERK2 (PDBID: 4GSB), where the side chains of E332^ERK2 and D334^ERK2 are disordered.