1rn7
From Proteopedia
(New page: 200px<br /> <applet load="1rn7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rn7, resolution 2.50Å" /> '''Structure of human ...) |
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| - | [[Image:1rn7.gif|left|200px]]<br /> | + | [[Image:1rn7.gif|left|200px]]<br /><applet load="1rn7" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1rn7" size=" | + | |
caption="1rn7, resolution 2.50Å" /> | caption="1rn7, resolution 2.50Å" /> | ||
'''Structure of human cystatin D'''<br /> | '''Structure of human cystatin D'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cystatins are natural inhibitors of papain-like (family C1) and | + | 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== | ==About this Structure== | ||
| - | 1RN7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1RN7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RN7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Abrahamson, M.]] | [[Category: Abrahamson, M.]] | ||
[[Category: Alvarez-Fernandez, M.]] | [[Category: Alvarez-Fernandez, M.]] | ||
| - | [[Category: Liang, Y | + | [[Category: Liang, Y H.]] |
| - | [[Category: Su, X | + | [[Category: Su, X D.]] |
[[Category: cystatin d]] | [[Category: cystatin d]] | ||
[[Category: inhibitor of cysteine peptidases]] | [[Category: inhibitor of cysteine peptidases]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:34 2008'' |
Revision as of 12:52, 21 February 2008
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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
1RN7 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
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