PDBsum entry 1cvz

Hydrolase

PDB id: 1cvz

Contents

Protein chain

212 a.a. *

Ligands

C48

Waters ×129

* Residue conservation analysis

References listed in PDB file

Key reference

• Title: Inhibition mechanism of cathepsin l-Specific inhibitors based on the crystal structure of papain-Clik148 complex.
• Authors: H.Tsuge, T.Nishimura, Y.Tada, T.Asao, D.Turk, V.Turk, N.Katunuma.
• Ref.: Biochem Biophys Res Commun, 1999, 266, 411-416. [DOI no: 10.1006/bbrc.1999.1830]
• PubMed id: 10600517

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.