2CIO
The high resolution x-ray structure of papain complexed with fragments of the Trypanosoma brucei cysteine protease inhibitor ICP.
Summary for 2CIO
| Entry DOI | 10.2210/pdb2cio/pdb |
| Related | 1BP4 1BQI 1CVZ 1EFF 1KHP 1KHQ 1PAD 1PE6 1PIP 1POP 1PPD 1PPN 1PPP 1STF 2PAD 4PAD 5PAD 6PAD 9PAP |
| Descriptor | PAPAIN, INHIBITOR OF CYSTEINE PEPTIDASE, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | hydrolase/inhibitor, complex hydrolase-inhibitor, icp, cysteine protease, inhibitor, trypanosoma brucei, allergen, protease, thiol protease, zymogen, hydrolase, hydrolase-inhibitor complex |
| Biological source | TRYPANOSOMA BRUCEI More |
| Total number of polymer chains | 2 |
| Total formula weight | 37309.84 |
| Authors | Alphey, M.S.,Hunter, W.N. (deposition date: 2006-03-24, release date: 2006-05-18, Last modification date: 2023-12-13) |
| Primary citation | Alphey, M.S.,Hunter, W.N. High-Resolution Complex of Papain with Remnants of a Cysteine Protease Inhibitor Derived from Trypanosoma Brucei Acta Crystallogr.,Sect.F, 62:504-, 2006 Cited by PubMed Abstract: Attempts to cocrystallize the cysteine protease papain derived from the latex of Carica papaya with an inhibitor of cysteine proteases (ICP) from Trypanosoma brucei were unsuccessful. However, crystals of papain that diffracted to higher resolution, 1.5 A, than other crystals of this archetypal cysteine protease were obtained, so the analysis was continued. Surprisingly, the substrate-binding cleft was occupied by two short peptide fragments which have been assigned as remnants of ICP. Comparisons reveal that these peptides bind in the active site in a manner similar to that of the human cysteine protease inhibitor stefin B when it is complexed to papain. The assignment of the fragment sequences is consistent with the specificity of the protease. PubMed: 16754967DOI: 10.1107/S1744309106014849 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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