Superposition of the inhibitor complexed structures of wild-type TACE (yellow) and a soakable form V353G TACE (differences are shown in blue). The mutation at position 353 stabilizes the enzyme from autoproteolysis and facilitates crystallization in a different space group that is amenable to inhibitor soaking and hence iterative structure-based drug design studies. The mutant protease retains enzymatic properties that are similar to those of the wild-type enzyme. Structural conformational changes are circled in red with the most dramatic change occurring within the loop from V353 to His361 (center circle)
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