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.
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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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:08:03 2008''
 
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Revision as of 19:43, 27 July 2008

File:2ch9.png

Template:STRUCTURE 2ch9

CRYSTAL STRUCTURE OF DIMERIC HUMAN CYSTATIN F

Template:ABSTRACT PUBMED 16601115

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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