1EF7

CRYSTAL STRUCTURE OF HUMAN CATHEPSIN X

Summary for 1EF7

• Entry DOI: 10.2210/pdb1ef7/pdb
• Descriptor: CATHEPSIN X (2 entities in total)
• Functional Keywords: papain-like, cysteine protease, carboxypeptidase, cathepsin, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Lysosome: Q9UBR2
• Total number of polymer chains: 2
• Total formula weight: 54354.19

Authors

Guncar, G.,Klemencic, I.,Turk, B.,Turk, V.,Karaoglanovic-Carmona, A.,Juliano, L.,Turk, D. (deposition date: 2000-02-07, release date: 2000-03-15, Last modification date: 2024-10-30)

Primary citation

Guncar, G.,Klemencic, I.,Turk, B.,Turk, V.,Karaoglanovic-Carmona, A.,Juliano, L.,Turk, D.
Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.
Structure Fold.Des., 8:305-313, 2000

PubMed Abstract: 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.

PubMed: 10745011
DOI: 10.1016/S0969-2126(00)00108-8

Experimental method

X-RAY DIFFRACTION (2.67 Å)