1m6d
From Proteopedia
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|PDB= 1m6d |SIZE=350|CAPTION= <scene name='initialview01'>1m6d</scene>, resolution 1.7Å | |PDB= 1m6d |SIZE=350|CAPTION= <scene name='initialview01'>1m6d</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=MYP:4-MORPHOLIN-4-YL-PIPERIDINE-1-CARBOXYLIC+ACID+[1-(3-BENZENESULFONYL-1-PROPYL-ALLYLCARBAMOYL)-2-PHENYLETHYL]-AMIDE'>MYP</scene> | + | |LIGAND= <scene name='pdbligand=MYP:4-MORPHOLIN-4-YL-PIPERIDINE-1-CARBOXYLIC+ACID+[1-(3-BENZENESULFONYL-1-PROPYL-ALLYLCARBAMOYL)-2-PHENYLETHYL]-AMIDE'>MYP</scene> |
- | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_F Cathepsin F], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.41 3.4.22.41] </span> | |
|GENE= CATF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CATF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6d OCA], [http://www.ebi.ac.uk/pdbsum/1m6d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m6d RCSB]</span> | ||
}} | }} | ||
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[[Category: Palmer, J T.]] | [[Category: Palmer, J T.]] | ||
[[Category: Somoza, J R.]] | [[Category: Somoza, J R.]] | ||
- | [[Category: MYP]] | ||
[[Category: papain family cysteine protease]] | [[Category: papain family cysteine protease]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:11:56 2008'' |
Revision as of 19:11, 30 March 2008
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, resolution 1.7Å | |||||||
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Ligands: | |||||||
Gene: | CATF (Homo sapiens) | ||||||
Activity: | Cathepsin F, with EC number 3.4.22.41 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of human cathepsin F
Overview
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.
About this Structure
1M6D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators., Somoza JR, Palmer JT, Ho JD, J Mol Biol. 2002 Sep 20;322(3):559-68. PMID:12225749
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