1CVZ
CRYSTAL STRUCTURE ANALYSIS OF PAPAIN WITH CLIK148(CATHEPSIN L SPECIFIC INHIBITOR)
Summary for 1CVZ
| Entry DOI | 10.2210/pdb1cvz/pdb |
| Descriptor | PAPAIN, N1-(1-DIMETHYLCARBAMOYL-2-PHENYL-ETHYL)-2-OXO-N4-(2-PYRIDIN-2-YL-ETHYL)-SUCCINAMIDE (3 entities in total) |
| Functional Keywords | papain, clik148, cathepsin l inhibitor, sulfhydryl proteinase, hydrolase |
| Biological source | Carica papaya (papaya) |
| Total number of polymer chains | 1 |
| Total formula weight | 23859.81 |
| Authors | Tsuge, H. (deposition date: 1999-08-24, release date: 2000-08-30, Last modification date: 2024-11-13) |
| Primary citation | Tsuge, H.,Nishimura, T.,Tada, Y.,Asao, T.,Turk, D.,Turk, V.,Katunuma, N. Inhibition mechanism of cathepsin L-specific inhibitors based on the crystal structure of papain-CLIK148 complex. Biochem.Biophys.Res.Commun., 266:411-416, 1999 Cited by PubMed Abstract: Papain was used as an experimental model structure to understand the inhibition mechanism of newly developed specific inhibitors of cathepsin L, the papain superfamily. Recently, we developed a series of cathepsin L-specific inhibitors which are called the CLIK series [(1999) FEBS Lett. 458, 6-10]. Here, we report the complex structure of papain with CLIK148, which is a representative inhibitor from the CLIK series. The inhibitor complex structure was solved at 1.7 A resolution with conventional R 0.177. Unlike other epoxisuccinate inhibitors (E64, CA030, and CA074), CLIK148 uses both prime and nonprime sites, which are important for the specific inhibitory effect on cathepsin L. Also, the specificity for cathepsin L could be explained by the existence of Phe in the P2 site and hydrophobic interaction of N-terminal pyridine ring. PubMed: 10600517DOI: 10.1006/bbrc.1999.1830 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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