2ch9
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(New page: 200px<br /> <applet load="2ch9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ch9, resolution 2.10Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 18:30, 29 October 2007
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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 ... [(full description)]
About this Structure
2CH9 is a [Single protein] structure of sequence from [Homo sapiens] with NAG, ZN and ACT as [ligands]. 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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