1fh0

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1fh0, resolution 1.6Å

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CRYSTAL STRUCTURE OF HUMAN CATHEPSIN V COMPLEXED WITH AN IRREVERSIBLE VINYL SULFONE INHIBITOR

Overview

Cathepsin V is a lysosomal cysteine protease that is expressed in the, thymus, testis and corneal epithelium. We have determined the 1.6 A, resolution crystal structure of human cathepsin V associated with an, irreversible vinyl sulfone inhibitor. The fold of this enzyme is similar, to the fold adopted by other members of the papain superfamily of cysteine, proteases. This study provides a framework for understanding the, structural basis for cathepsin V's activity and will aid in the design of, inhibitors of this enzyme. A comparison of cathepsin V's active site with, the active sites of related proteases revealed a number of differences, especially in the S2 and S3 subsites, that could be exploited in, identifying specific cathepsin V inhibitors or in identifying inhibitors, of other cysteine proteases that would be selective against cathepsin V.

About this Structure

1FH0 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of human cathepsin V., Somoza JR, Zhan H, Bowman KK, Yu L, Mortara KD, Palmer JT, Clark JM, McGrath ME, Biochemistry. 2000 Oct 17;39(41):12543-51. PMID:11027133

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