Homology model of pancreasin. A model of the predicted pancreasin catalytic domain was generated starting from the crystallographically derived structure of human  II-tryptase. The propeptide and the carboxyl-terminal 11?residues of pancreasin were omitted because they have no counterpart in the tryptase structure. In the model shown, the catalytic triad residues (His-75, Asp-124, Ser-229) in the active site are red, basic residues (lysine and arginine) are blue, acidic residues (aspartate and glutamate) are green, and predicted N-linked carbohydrate (CHO) attachment sites (Asn-55 and Asn-89) are cyan. Note that sugars (not shown) attached to Asn-55 and Asn-89 could influence access and binding of substrates in the active site. The ribbon structure shows side chains of the catalytic triad residues and putative N-linked asparagines. "Front" views show the active site face one, with the extended substrate-binding site oriented roughly vertically. "Side" views depict the active site binding cleft in profile, with the carbohydrate attachment sites to the left. The distribution of surface side chains of basic and acidic residues suggests patches of positive charge, despite an overall excess of residues with acidic side chains. J. Biol. Chem., Vol. 278, Issue 5, 3363-3371, January 31, 2003 |