1FH0

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

Summary for 1FH0

• Entry DOI: 10.2210/pdb1fh0/pdb
• Related PRD ID: PRD_000325
• Descriptor: CATHEPSIN V, Nalpha-[(4-methylpiperazin-1-yl)carbonyl]-N-[(3S)-1-phenyl-5-(phenylsulfonyl)pentan-3-yl]-L-phenylalaninamide, SULFATE ION, ... (4 entities in total)
• Functional Keywords: cathepsin, papain, protease, cancer, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Lysosome : O60911
• Total number of polymer chains: 2
• Total formula weight: 49331.48

Authors

Somoza, J.R. (deposition date: 2000-07-30, release date: 2001-07-30, Last modification date: 2024-11-20)

Primary citation

Somoza, J.R.,Zhan, H.,Bowman, K.K.,Yu, L.,Mortara, K.D.,Palmer, J.T.,Clark, J.M.,McGrath, M.E.
Crystal structure of human cathepsin V.
Biochemistry, 39:12543-12551, 2000

PubMed Abstract: 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.

PubMed: 11027133
DOI: 10.1021/bi000951p

Experimental method

X-RAY DIFFRACTION (1.6 Å)