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New page: left|200px<br /> <applet load="1roa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1roa, resolution 1.80Å" /> '''Structure of human ...
 
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[[Image:1roa.gif|left|200px]]<br />
<applet load="1roa" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1roa, resolution 1.80&Aring;" />
'''Structure of human cystatin D'''<br />


==Overview==
==Structure of human cystatin D==
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 &gt; cathepsin H &gt;, 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.
<StructureSection load='1roa' size='340' side='right'caption='[[1roa]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1roa]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ROA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1roa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1roa OCA], [https://pdbe.org/1roa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1roa RCSB], [https://www.ebi.ac.uk/pdbsum/1roa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1roa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYTD_HUMAN CYTD_HUMAN] Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B.<ref>PMID:8083219</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/1roa_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1roa ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 &gt; cathepsin H &gt; 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==
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<ref>PMID:15728581</ref>
1ROA 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ROA OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15728581 15728581]
</div>
<div class="pdbe-citations 1roa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Abrahamson, M.]]
[[Category: Abrahamson M]]
[[Category: Alvarez-Fernandez, M.]]
[[Category: Alvarez-Fernandez M]]
[[Category: Liang, Y.H.]]
[[Category: Liang YH]]
[[Category: Su, X.D.]]
[[Category: Su XD]]
[[Category: cystatin d]]
[[Category: inhibitor of cysteine pepidases]]
 
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