1mir
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RAT PROCATHEPSIN B
OverviewOverview
BACKGROUND: Cysteine proteases of the papain superfamily are synthesized, as inactive precursors with a 60-110 residue N-terminal prosegment. The, propeptides are potent inhibitors of their parent proteases. Although the, proregion binding mode has been elucidated for all other protease classes, that of the cysteine proteases remained elusive. RESULTS: We report the, three-dimensional structure of rat procathepsin B, determined at 2.8 A, resolution. The 62-residue proregion does not form a globular structure on, its own, but folds along the surface of mature cathepsin B. The N-terminal, part of the proregion packs against a surface loop, with Trp24p (p, indicating the proregion) playing a pivotal role in these interactions., Inhibition occurs by blocking access to the active site: part of ... [(full description)]
About this StructureAbout this Structure
1MIR is a [Single protein] structure of sequence from [Rattus norvegicus]. Active as [Cathepsin B], with EC number [3.4.22.1]. Structure known Active Sites: CYA and CYB. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion., Cygler M, Sivaraman J, Grochulski P, Coulombe R, Storer AC, Mort JS, Structure. 1996 Apr 15;4(4):405-16. PMID:8740363
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