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3ul5

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==Saccharum officinarum canecystatin-1 in space group C2221==
==Saccharum officinarum canecystatin-1 in space group C2221==
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<StructureSection load='3ul5' size='340' side='right' caption='[[3ul5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='3ul5' size='340' side='right'caption='[[3ul5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ul5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sacof Sacof]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UL5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UL5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ul5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharum_officinarum Saccharum officinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UL5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ul6|3ul6]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cystatin-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4547 SACOF])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ul5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ul5 OCA], [https://pdbe.org/3ul5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ul5 RCSB], [https://www.ebi.ac.uk/pdbsum/3ul5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ul5 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ul5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ul5 OCA], [http://pdbe.org/3ul5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ul5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ul5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ul5 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q7Y0Q9_SACOF Q7Y0Q9_SACOF]
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The three dimensional structure of canecystatin-1, a potent inhibitor of cysteine proteases from sugar cane (Saccharum officinarum), has been solved in two different crystal forms. In both cases it is seen to exist as a domain-swapped dimer, the first such observation for a cystatin of plant origin. Size exclusion chromatography and multi-dimensional NMR spectroscopy show the dimer to be the dominant species in solution, despite the presence of a measurable quantity of monomer undergoing slow exchange. The latter is believed to be the active species whilst the domain-swapped dimer is presumably inactive as its first inhibitory loop has been extended to form part of a long beta-strand which forms a double-helical coiled coil with its partner from the other monomer. A similar structure is observed in human cystatin C but the spatial disposition of the two lobes of the dimer is rather different. Dimerization is presumably a mechanism by which canecystatin-1 can be maintained inactive within the plant avoiding the inhibition of endogenous proteases. The structure described here provides a platform for rationally designing specific cysteine protease inhibitors for biotechnological applications. (c) 2012 The Authors Journal compilation (c) 2012 FEBS.
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X-ray crystallography and NMR studies of domain-swapped canecystatin-1.,Valadares NF, de Oliveira-Silva R, Cavini IA, de Almeida Marques I, Pereira HD, Soares-Costa A, Henrique-Silva F, Kalbitzer HR, Munte CE, Garratt RC FEBS J. 2012 Dec 14. doi: 10.1111/febs.12095. PMID:23241243<ref>PMID:23241243</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ul5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Sacof]]
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[[Category: Large Structures]]
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[[Category: Garratt, R C]]
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[[Category: Saccharum officinarum]]
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[[Category: Oliveira-Silva, R]]
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[[Category: Garratt RC]]
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[[Category: Pereira, H M]]
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[[Category: Oliveira-Silva R]]
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[[Category: Valadares, N F]]
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[[Category: Pereira HM]]
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[[Category: Cystatin]]
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[[Category: Valadares NF]]
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[[Category: Defense]]
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[[Category: Hydrolase inhibitor]]
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Current revision

Saccharum officinarum canecystatin-1 in space group C2221

PDB ID 3ul5

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