2ch9: Difference between revisions

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[[Image:2ch9.gif|left|200px]]
{{Seed}}
[[Image:2ch9.png|left|200px]]


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{{STRUCTURE_2ch9|  PDB=2ch9  |  SCENE=  }}  
{{STRUCTURE_2ch9|  PDB=2ch9  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF DIMERIC HUMAN CYSTATIN F'''
===CRYSTAL STRUCTURE OF DIMERIC HUMAN CYSTATIN F===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_16601115}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_16601115}}


==About this Structure==
==About this Structure==
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[[Category: N-linked glycan]]
[[Category: N-linked glycan]]
[[Category: Thiol protease inhibitor]]
[[Category: Thiol protease inhibitor]]
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