1rn7
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(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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Revision as of 16:59, 12 November 2007
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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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