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PDBsum entry 1sp4
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Hydrolase/hydrolase inhibitor
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PDB id
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1sp4
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of ns-134 in complex with bovine cathepsin b: a two-Headed epoxysuccinyl inhibitor extends along the entire active-Site cleft.
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Authors
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I.Stern,
N.Schaschke,
L.Moroder,
D.Turk.
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Ref.
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Biochem J, 2004,
381,
511-517.
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PubMed id
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Abstract
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The crystal structure of the inhibitor NS-134 in complex with bovine cathepsin B
reveals that functional groups attached to both sides of the epoxysuccinyl
reactive group bind to the part of active-site cleft as predicted. The
-Leu-Pro-OH side binds to the primed binding sites interacting with the His110
and His111 residues with its C-terminal carboxy group, whereas the -Leu-Gly-Meu
(-Leu-Gly-Gly-OMe) part (Meu, methoxycarbonylmethyl) binds along the non-primed
binding sites. Comparison with the propeptide structures of cathepsins revealed
that the binding of the latter part is least similar to the procathepsin B
structure; this result, together with the two-residue shift in positioning of
the Leu-Gly-Gly part, suggests that the propeptide structures of the cognate
enzymes may not be the best starting point for the design of reverse binding
inhibitors.
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