1cvz

CRYSTAL STRUCTURE ANALYSIS OF PAPAIN WITH CLIK148(CATHEPSIN L SPECIFIC INHIBITOR)

spinqualitylabelsall models 1cvz, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1cvz is a 1 chain structure with sequence from Carica papaya. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: C48 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PAPA1_CARPA Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Inhibition mechanism of cathepsin L-specific inhibitors based on the crystal structure of papain-CLIK148 complex.,Tsuge H, Nishimura T, Tada Y, Asao T, Turk D, Turk V, Katunuma N Biochem Biophys Res Commun. 1999 Dec 20;266(2):411-6. PMID:10600517 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Papain

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