2ch9: Difference between revisions
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[[Image:2ch9.gif|left|200px]] | [[Image:2ch9.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF DIMERIC HUMAN CYSTATIN F''' | {{Structure | ||
|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> | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF DIMERIC HUMAN CYSTATIN F''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2CH9 is a [ | 2CH9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CH9 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16601115 16601115] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thiol protease inhibitor]] | [[Category: thiol protease inhibitor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:15:20 2008'' | ||
Revision as of 14:15, 20 March 2008
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| 2ch9, resolution 2.10Å | |||||||||||||
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| Sites: | AC6 | ||||||||||||
| Ligands: | NAG, ZN and ACT | ||||||||||||
| 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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