1qdq
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X-RAY CRYSTAL STRUCTURE OF BOVINE CATHEPSIN B-CA074 COMPLEX
OverviewOverview
The crystal structure of the bovine spleen cathepsin B (BSCB)-CA074, complex was refined to R = 0.152 using X-ray diffraction data up to 2.18 A, resolution. BSCB is characterized by an extra Cys148-Cys252 disulfide, bridge, as compared with rat and human CBs. Although the crystal, structures of these enzymes showed similar overall folding, a difference, was observed in the occluding loop, a structural element specific only to, CB. Comparison of the torsion angles indicated the different flexibilities, of their loop structures. The oxirane C6 atom of CA074 was covalently, bonded to the Cys29 S(gamma) atom (C3-S(gamma)=1.81 A), where the, S-configuration was transformed to the R-form. Concerning the oxirane, carbon atom that participates in the covalent bonding with the Cys, residue, an acceptable rule has been proposed. The substrate specificities, at the Sn (n = 1-3) and Sn' (n=1 and 2) subsites of CB, together with the, interaction features as to CA074, have been discussed in comparison with, the crystal structure of the papain-CA028 (a CA074-related inhibitor), complex.
About this StructureAbout this Structure
1QDQ is a Single protein structure of sequence from Bos taurus with 074 as ligand. Active as Cathepsin B, with EC number 3.4.22.1 Full crystallographic information is available from OCA.
ReferenceReference
Substrate specificity of bovine cathepsin B and its inhibition by CA074, based on crystal structure refinement of the complex., Yamamoto A, Tomoo K, Hara T, Murata M, Kitamura K, Ishida T, J Biochem (Tokyo). 2000 Apr;127(4):635-43. PMID:10739956
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