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1pbh
From Proteopedia
| 1pbh, resolution 3.20Å () | |||||||||
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| Activity: | Cathepsin B, with EC number 3.4.22.1 | ||||||||
| Domains: | Propeptide_C1, Peptidase_C1A_CathepsinB | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
CRYSTAL STRUCTURE OF HUMAN RECOMBINANT PROCATHEPSIN B AT 3.2 ANGSTROM RESOLUTION
A wild-type human procathepsin B was expressed, crystallized in two crystal forms and its crystal structure determined at 3.2 and 3.3 Angstroms resolution. The structure reveals that the propeptide folds on the cathepsin B surface, shielding the enzyme active site from exposure to solvent. The structure of the enzymatically active domains is virtually identical to that of the native enzyme [Musil et al. (1991) EMBO J. 10, 2321-2330]: the main difference is that the occluding loop residues are lifted above the body of the mature enzyme, supporting the propeptide structure.
Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide., Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V, FEBS Lett. 1996 Apr 22;384(3):211-4. PMID:8617355
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1PBH is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Turk D, Podobnik M, Kuhelj R, Dolinar M, Turk V. Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett. 1996 Apr 22;384(3):211-4. PMID:8617355
Page seeded by OCA on Wed Feb 18 02:28:08 2009
