1ef7: Difference between revisions
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cathepsin_X Cathepsin X], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.18.1 3.4.18.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_X Cathepsin X], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.18.1 3.4.18.1] </span> | ||
|GENE= | |GENE= | ||
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ef7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ef7 OCA], [http://www.ebi.ac.uk/pdbsum/1ef7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ef7 RCSB]</span> | |||
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[[Category: papain-like]] | [[Category: papain-like]] | ||
''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 20:01:35 2008'' | ||
Revision as of 20:01, 30 March 2008
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| , resolution 2.67Å | |||||||
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| Activity: | Cathepsin X, with EC number 3.4.18.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN CATHEPSIN X
OverviewOverview
BACKGROUND: Cathepsin X is a widespread, abundantly expressed papain-like mammalian lysosomal cysteine protease. It exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity and shares a similar activity profile with cathepsin B. The latter has been implicated in normal physiological events as well as in various pathological states such as rheumatoid arthritis, Alzheimer's disease and cancer progression. Thus the question is raised as to which of the two enzyme activities has actually been monitored. RESULTS: The crystal structure of human cathepsin X has been determined at 2.67 A resolution. The structure shares the common features of a papain-like enzyme fold, but with a unique active site. The most pronounced feature of the cathepsin X structure is the mini-loop that includes a short three-residue insertion protruding into the active site of the protease. The residue Tyr27 on one side of the loop forms the surface of the S1 substrate-binding site, and His23 on the other side modulates both carboxy-monopeptidase as well as carboxy-dipeptidase activity of the enzyme by binding the C-terminal carboxyl group of a substrate in two different sidechain conformations. CONCLUSIONS: The structure of cathepsin X exhibits a binding surface that will assist in the design of specific inhibitors of cathepsin X as well as of cathepsin B and thereby help to clarify the physiological roles of both proteases.
About this StructureAbout this Structure
1EF7 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease., Guncar G, Klemencic I, Turk B, Turk V, Karaoglanovic-Carmona A, Juliano L, Turk D, Structure. 2000 Mar 15;8(3):305-13. PMID:10745011
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