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2ch9
From Proteopedia
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|PDB= 2ch9 |SIZE=350|CAPTION= <scene name='initialview01'>2ch9</scene>, resolution 2.10Å | |PDB= 2ch9 |SIZE=350|CAPTION= <scene name='initialview01'>2ch9</scene>, resolution 2.10Å | ||
|SITE= <scene name='pdbsite=AC6:Zn+Binding+Site+For+Chain+A'>AC6</scene> | |SITE= <scene name='pdbsite=AC6:Zn+Binding+Site+For+Chain+A'>AC6</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ch9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ch9 OCA], [http://www.ebi.ac.uk/pdbsum/2ch9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ch9 RCSB]</span> | ||
}} | }} | ||
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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: ACT]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: ZN]] | ||
[[Category: cystatin f activation]] | [[Category: cystatin f activation]] | ||
[[Category: cysteine protease inhibtion]] | [[Category: cysteine protease inhibtion]] | ||
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[[Category: thiol protease inhibitor]] | [[Category: thiol protease inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:21:26 2008'' |
Revision as of 23:21, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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