1pci
From Proteopedia
(New page: 200px<br /> <applet load="1pci" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pci, resolution 3.2Å" /> '''PROCARICAIN'''<br />...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1PCI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Carica_papaya Carica papaya]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.6 3.4.22.6]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PCI OCA]]. | + | 1PCI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Carica_papaya Carica papaya]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.6 3.4.22.6]]. Structure known Active Sites: ACA, ACB and ACC. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PCI OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: zymogen]] | [[Category: zymogen]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:27:15 2007'' |
Revision as of 06:22, 30 October 2007
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PROCARICAIN
Overview
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 Structure
1PCI is a [Single protein] structure of sequence from [Carica papaya]. Active as [Hydrolase], with EC number [3.4.22.6]. Structure known Active Sites: ACA, ACB and ACC. Full crystallographic information is available from [OCA].
Reference
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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