1pci: Difference between revisions

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[[Category: zymogen]]
[[Category: zymogen]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:21:42 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:58:37 2007''

Revision as of 16:53, 30 October 2007

File:1pci.gif


1pci, resolution 3.2Å

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PROCARICAIN

OverviewOverview

BACKGROUND: 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. RESULTS: The crystal structure of, procaricain has been refined to 3.2 A resolution; the final model ... [(full description)]

About this StructureAbout this Structure

1PCI is a [Single protein] structure of sequence from [Carica papaya]. Active as [Chymopapain], with EC number [3.4.22.6]. Structure known Active Sites: ACA, ACB and ACC. Full crystallographic information is available from [OCA].

ReferenceReference

The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft., Groves MR, Taylor MA, Scott M, Cummings NJ, Pickersgill RW, Jenkins JA, Structure. 1996 Oct 15;4(10):1193-203. PMID:8939744

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OCA