The NMR structure of the inhibited catalytic domain of human stromelysin−1

The three−dimensional structure of the catalytic domain of stromelysin−1 complexed with an N−carboxyl alkyl inhibitor has been determined by NMR methods. The global fold consists of three helices, a five stranded −sheet and a methionine located in a turn near the catalytic histidines, classifying stromelysin−1 as a metzincin. Stromelysin−1 is unique in having two independent zinc binding sites: a catalytic site and a structural site. The inhibitor binds in an extended conformation. The S1' subsite is a deep hydrophobic pocket, whereas S2' appears shallow and S3' open.

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