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2ch9
From Proteopedia
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[[Image:2ch9.gif|left|200px]] | [[Image:2ch9.gif|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF DIMERIC HUMAN CYSTATIN F''' | '''CRYSTAL STRUCTURE OF DIMERIC HUMAN CYSTATIN F''' | ||
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[[Category: Aalten, D M.F Van.]] | [[Category: Aalten, D M.F Van.]] | ||
[[Category: Schuettelkopf, A W.]] | [[Category: Schuettelkopf, A W.]] | ||
| - | [[Category: | + | [[Category: Cystatin f activation]] |
| - | [[Category: | + | [[Category: Cysteine protease inhibtion]] |
| - | [[Category: | + | [[Category: Glycoprotein]] |
| - | [[Category: | + | [[Category: N-linked glycan]] |
| - | [[Category: | + | [[Category: Thiol protease inhibitor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:08:03 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:08, 3 May 2008
CRYSTAL STRUCTURE OF DIMERIC HUMAN CYSTATIN F
Overview
Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase. Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes. It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile. We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state. The two monomers interact in a fashion not seen before for cystatins or cystatin-like proteins that is crucially dependent on an unusual intermolecular disulfide bridge, suggesting how reduction leads to monomer formation and activation. Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
About this Structure
2CH9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis of reduction-dependent activation of human cystatin F., Schuttelkopf AW, Hamilton G, Watts C, van Aalten DM, J Biol Chem. 2006 Jun 16;281(24):16570-5. Epub 2006 Apr 6. PMID:16601115 Page seeded by OCA on Sat May 3 22:08:03 2008
