The recent development in the structure-function relationship of pancreatic
phospholipase A(2) is reviewed. The results of extensive studies by a comb
ination of site-directed mutagenesis, X-ray crystallography, and NMR have p
rovided new insight into several old issues. In particular, we summarize cu
rrent views on the active site, the interfacial binding site, the mechanism
of interfacial activation, the roles of the hydrogen-bonding network and t
he catalytic dyad, and the conformational stability of the structure. (C) 1
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