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1MIR

RAT PROCATHEPSIN B

Summary for 1MIR
Entry DOI10.2210/pdb1mir/pdb
DescriptorPROCATHEPSIN B (2 entities in total)
Functional Keywordshydrolase, thiol protease, cysteine protease
Biological sourceRattus norvegicus (Norway rat)
Total number of polymer chains2
Total formula weight71267.25
Authors
Cygler, M.,Sivaraman, J.,Grochulski, P.,Coulombe, R.,Storer, A.C.,Mort, J.S. (deposition date: 1996-01-12, release date: 1997-01-11, Last modification date: 2024-10-30)
Primary citationCygler, M.,Sivaraman, J.,Grochulski, P.,Coulombe, R.,Storer, A.C.,Mort, J.S.
Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion.
Structure, 4:405-416, 1996
Cited by
PubMed Abstract: 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.
PubMed: 8740363
DOI: 10.1016/S0969-2126(96)00046-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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