1M6D

Crystal structure of human cathepsin F

Summary for 1M6D

• Entry DOI: 10.2210/pdb1m6d/pdb
• Descriptor: Cathepsin F, 4-MORPHOLIN-4-YL-PIPERIDINE-1-CARBOXYLIC ACID [1-(3-BENZENESULFONYL-1-PROPYL-ALLYLCARBAMOYL)-2-PHENYLETHYL]-AMIDE (3 entities in total)
• Functional Keywords: papain family cysteine protease, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Lysosome: Q9UBX1
• Total number of polymer chains: 2
• Total formula weight: 48480.81

Authors

Somoza, J.R.,Palmer, J.T.,Ho, J.D. (deposition date: 2002-07-15, release date: 2003-07-15, Last modification date: 2024-12-25)

Primary citation

Somoza, J.R.,Palmer, J.T.,Ho, J.D.
The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators
J.Mol.Biol., 322:559-568, 2002

PubMed Abstract: Cathepsin F is a lysosomal cysteine protease of the papain family, and likely plays a regulatory role in processing the invariant chain that is associated with the major histocompatibility complex (MHC) class II. Evidence suggests that inhibiting cathepsin F activity will block MHC class II processing in macrophages. Consequently, inhibitors of this enzyme may be useful in treating certain diseases that involve an inappropriate or excessive immune response. We have determined the 1.7A structure of the mature domain of human cathepsin F associated with an irreversible vinyl sulfone inhibitor. This structure provides a basis for understanding cathepsin F's substrate specificity, and suggests ways of identifying potent and selective inhibitors of this enzyme.

PubMed: 12225749
DOI: 10.1016/S0022-2836(02)00780-5

Experimental method

X-RAY DIFFRACTION (1.7 Å)