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. 2015 Aug;56(8):1386–1402. doi: 10.1194/jlr.R057588

Fig. 2.

Fig. 2.

Ribbon diagram of cPLA2α structure. Two ions of calcium bind to the calcium-binding loops (CBL) on the membrane binding face of the C2 domain. The catalytic domain with the active site nucleophile S228 contains residues involved in cPLA2α regulation (pink) that include phosphorylation sites (S505, S727), basic residues (K488, K544, K543), and W464 important for membrane interaction. The residues mutated in humans with cPLA2α deficiencies are shown in yellow. The residue V707 is predicted to be the start of the deletion in patients with cryptogenic multifocal ulcerating stenosing enteritis.