THE CYSTEINE PROTEASE CRUZAIN BOUND TO WRR-204
N-[N'-BENZYLOXYCARBONYL-PHENYLALANINYL]-3-AMINO-5-PHENYL-PENTANE-1-SULFONIC ACID PHENYL ESTER
Crystal Structure of Cruzain bound to WRR-204
University of California, San Francisco (THESIS)
Enzyme-ligand Interactions, Inhibition and Specificity
Chapter 3: X-ray Structures of Complexes of Cruzain with Designed Covalent Inhibitors
Structural Determinants of Specificity in the Cysteine Protease Cruzain
The Crystal Structure of Cruzain: a Therapeutic Target for Chagas' Disease
APAAVDWRARGAVTAVKDQGQCGSCWAFSAIGNVECQWFLAGHPLTNLSEQMLVSCDKTDSGCSGGLMNNAFEWIVQENN GAVYTEDSYPYASGEGISPPCTTSGHTVGATITGHVELPQDEAQIAAWLAVNGPVAVAVDASSWMTYTGGVMTSCVSEQL DHGVLLVGYNDSAAVPYWIIKNSWTTQWGEEGYIRIAKGSNQCLVKEEASSAVVG
0.8M NaCitrate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 292K
VSC WAS N-[N'-BENZYLOXYCARBONYL-PHENYLALANINYL]-3-AMINO- 5-PHENYL-PENT-1-ENE-1-SULFONIC ACID PHENYL ESTER BEFORE REACTION WITH THE PROTEASE. AFTER REACTION, THE SG OF CYS 25 IS LINKED TO C32 OF THE VSC 280, N-[N'-BENZYLOXYCARBONYL-PHENYLALANINYL]-3-AMINO-5- PHENYL-PENTANE-1-SULFONIC ACID PHENYL ESTER. THE PHENYL RING ATTACHED TO ONE OXYGEN OF THE SULFONIC ACID PORTION OF THE LIGAND IS MISSING IN THE DENSITY.
THERE IS A STOP CODON AFTER RESIDUE 212.
cysteine protease, drug design, covalent inhibitor, cruzipain, HYDROLASE-HYDROLASE INHIBITOR COMPLEX