Inherited human cPLA_2α deficiency is associated with impaired eicosanoid biosynthesis, small intestinal ulceration, and platelet dysfunction
J. Clin. Invest. David H. Adler, et al. 118:2121 doi:10.1172/JCI30473 [Go to this article.]

Figure 10
Effects of histidine substitution at residue 485 of cPLA_2α. Comparison of the wild-type cPLA_2α structure (left) with a model of the p.[R485H] mutation (right). Backbone trace is shown in gray with the backbone of positively charged positions shown in blue and labeled with a plus sign; the capping helix is highlighted in purple. Oxygen atoms and hydroxy groups are shown in red, nitrogen atoms in blue, and sulfur atoms in yellow. The side-chain carbon atoms of the 485 position are shown in green, and the side-chain atoms of catalytically important residues are highlighted in yellow. Hydrogen bonds are indicated with a dashed black line while distances too long to form a hydrogen-bonding interaction are shown with solid blue lines. Modeling of histidine into position 485 reveals that 2 ideal hydrogen bonds between the side chain of p.[R485] and the backbone carbonyl of p.[T481] and side-chain Sγ of p.[M470] are lost. This mutation is predicted to introduce a destabilizing cavity in the location of the p.[R485] side chain.