1roa
From Proteopedia
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'''Structure of human cystatin D''' | '''Structure of human cystatin D''' | ||
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[[Category: Liang, Y H.]] | [[Category: Liang, Y H.]] | ||
[[Category: Su, X D.]] | [[Category: Su, X D.]] | ||
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Revision as of 04:43, 3 May 2008
Structure of human cystatin D
Overview
Cystatins are natural inhibitors of papain-like (family C1) and legumain-related (family C13) cysteine peptidases. Cystatin D is a type 2 cystatin, a secreted inhibitor found in human saliva and tear fluid. Compared with its homologues, cystatin D presents an unusual inhibition profile with a preferential inhibition cathepsin S > cathepsin H > cathepsin L and no inhibition of cathepsin B or pig legumain. To elucidate the structural reasons for this specificity, we have crystallized recombinant human Arg(26)-cystatin D and solved its structures at room temperature and at cryo conditions to 2.5- and 1.8-A resolution, respectively. Human cystatin D presents the typical cystatin fold, with a five-stranded anti-parallel beta-sheet wrapped around a five-turn alpha-helix. The structures reveal differences in the peptidase-interacting regions when compared with other cystatins, providing plausible explanations for the restricted inhibitory specificity of cystatin D for some papain-like peptidases and its lack of reactivity toward legumain-related enzymes.
About this Structure
1ROA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile., Alvarez-Fernandez M, Liang YH, Abrahamson M, Su XD, J Biol Chem. 2005 May 6;280(18):18221-8. Epub 2005 Feb 23. PMID:15728581 Page seeded by OCA on Sat May 3 07:43:30 2008
