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2ch9
From Proteopedia
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| - | [[Image:2ch9.gif|left|200px]]<br /><applet load="2ch9" size=" | + | [[Image:2ch9.gif|left|200px]]<br /><applet load="2ch9" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ch9, resolution 2.10Å" /> | caption="2ch9, resolution 2.10Å" /> | ||
'''CRYSTAL STRUCTURE OF DIMERIC HUMAN CYSTATIN F'''<br /> | '''CRYSTAL STRUCTURE OF DIMERIC HUMAN CYSTATIN F'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG, ZN and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC6:Zn Binding Site For Chain A'>AC6</scene>. Full crystallographic information is available from [http:// | + | 2CH9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC6:Zn+Binding+Site+For+Chain+A'>AC6</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CH9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thiol protease inhibitor]] | [[Category: thiol protease inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:35:18 2008'' |
Revision as of 08:35, 3 February 2008
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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 with , and as ligands. Known structural/functional Site: . 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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