1F29

CRYSTAL STRUCTURE ANALYSIS OF CRUZAIN BOUND TO A VINYL SULFONE DERIVED INHIBITOR (I)

Summary for 1F29

• Entry DOI: 10.2210/pdb1f29/pdb
• Related: 1AIM 1EWL 1EWM 1EWO 1EWP 1F2A 1F2B 1F2C 2AIM
• Descriptor: CRUZAIN, 3-[[N-[MORPHOLIN-N-YL]-CARBONYL]-PHENYLALANINYL-AMINO]-5- PHENYL-PENTANE-1-SULFONYLBENZENE (3 entities in total)
• Functional Keywords: cysteine protease, covalent inhibitor, vinyl sulfone derived, p1' pocket, hydrolase
• Biological source: Trypanosoma cruzi
• Total number of polymer chains: 3
• Total formula weight: 69836.52

Authors

Brinen, L.S.,Hansell, E.,Roush, W.R.,McKerrow, J.H.,Fletterick, R.J. (deposition date: 2000-05-23, release date: 2000-07-26, Last modification date: 2024-10-16)

Primary citation

Brinen, L.S.,Hansell, E.,Cheng, J.,Roush, W.R.,McKerrow, J.H.,Fletterick, R.J.
A target within the target: probing cruzain's P1' site to define structural determinants for the Chagas' disease protease.
Structure Fold.Des., 8:831-840, 2000

PubMed Abstract: Cysteine proteases of the papain superfamily are present in nearly all groups of eukaryotes and play vital roles in a wide range of biological processes and diseases, including antigen and hormone processing, bacterial infection, arthritis, osteoporosis, Alzheimer's disease and cancer-cell invasion. Because they are critical to the life-cycle progression of many pathogenic protozoa, they represent potential targets for selective inhibitors. Chagas' disease, the leading cause of death due to heart disease in Latin American countries, is transmitted by Trypanosoma cruzi. Cruzain is the major cysteine protease of T cruzi and has been the target of extensive structure-based drug design.

PubMed: 10997902
DOI: 10.1016/S0969-2126(00)00173-8

Experimental method

X-RAY DIFFRACTION (2.15 Å)