1sp4
From Proteopedia
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Crystal structure of NS-134 in complex with bovine cathepsin B: a two headed epoxysuccinyl inhibitor extends along the whole active site cleft
Overview
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.
About this Structure
1SP4 is a Protein complex structure of sequences from Bos taurus with EPO, LEU and PRO as ligands. Active as Cathepsin B, with EC number 3.4.22.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of NS-134 in complex with bovine cathepsin B: a two-headed epoxysuccinyl inhibitor extends along the entire active-site cleft., Stern I, Schaschke N, Moroder L, Turk D, Biochem J. 2004 Jul 15;381(Pt 2):511-7. PMID:15084146
Page seeded by OCA on Wed Nov 21 02:32:24 2007
