1roa
From Proteopedia
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| - | [[Image:1roa.gif|left|200px]] | + | [[Image:1roa.gif|left|200px]] |
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| - | '''Structure of human cystatin D''' | + | {{Structure |
| + | |PDB= 1roa |SIZE=350|CAPTION= <scene name='initialview01'>1roa</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Structure of human cystatin D''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ROA is a [ | + | 1ROA is a [[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=1ROA OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15728581 15728581] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Su, X D.]] | [[Category: Su, X D.]] | ||
[[Category: cystatin d]] | [[Category: cystatin d]] | ||
| - | [[Category: inhibitor of cysteine | + | [[Category: inhibitor of cysteine pepidase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:54:12 2008'' |
Revision as of 11:54, 20 March 2008
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| , resolution 1.80Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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