1PCI
PROCARICAIN
Summary for 1PCI
Entry DOI | 10.2210/pdb1pci/pdb |
Descriptor | PROCARICAIN (1 entity in total) |
Functional Keywords | zymogen, hydrolase, thiol protease |
Biological source | Carica papaya (papaya) |
Total number of polymer chains | 3 |
Total formula weight | 107820.98 |
Authors | Groves, M.R.,Taylor, M.A.J.,Scott, M.,Cummings, N.J.,Pickersgill, R.W.,Jenkins, J.A. (deposition date: 1996-06-28, release date: 1997-04-01, Last modification date: 2023-08-09) |
Primary citation | Groves, M.R.,Taylor, M.A.,Scott, M.,Cummings, N.J.,Pickersgill, R.W.,Jenkins, J.A. The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft. Structure, 4:1193-1203, 1996 Cited by PubMed Abstract: Cysteine proteases are involved in a variety of cellular processes including cartilage degradation in arthritis, the progression of Alzheimer's disease and cancer invasion: these enzymes are therefore of immense biological importance. Caricain is the most basic of the cysteine proteases found in the latex of Carica papaya. It is a member of the papain superfamily and is homologous to other plant and animal cysteine proteases. Caricain is naturally expressed as an inactive zymogen called procaricain. The inactive form of the protease contains an inhibitory proregion which consists of an additional 106 N-terminal amino acids; the proregion is removed upon activation. PubMed: 8939744DOI: 10.1016/S0969-2126(96)00127-X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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