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| [[Image:1rn7.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1rn7| PDB=1rn7 | SCENE= }} | | {{STRUCTURE_1rn7| PDB=1rn7 | SCENE= }} |
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| '''Structure of human cystatin D'''
| | ===Structure of human cystatin D=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15728581}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15728581 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15728581}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Cystatin d]] | | [[Category: Cystatin d]] |
| [[Category: Inhibitor of cysteine peptidase]] | | [[Category: Inhibitor of cysteine peptidase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:41:29 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:39:12 2008'' |
