Article
The contribution of key hydrophobic residues in ecotin to enzyme-inhibitor complex stability.
Journal of enzyme inhibition and medicinal chemistry - 1 Dec 2009
McCrudden Maelíosa T C, Ryan Louise A, Turkington Philip, Timson David J
Abstract excerpt
The Escherichia coli protease inhibitor ecotin is believed to be implicated in the evasion of host defenses during infection. The protein has also attracted attention as a scaffold for the design of novel, specific protease inhibitors. Ecotin interacts with its targets through two sites. Key hydrophobic residues in both sites (Leu-64, Trp-67, Tyr-69, Met-84, and Met-85) were mutated to alanine and the effects on...
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