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3ul5
From Proteopedia
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| - | + | ==Saccharum officinarum canecystatin-1 in space group C2221== | |
| - | ===Saccharum officinarum | + | <StructureSection load='3ul5' size='340' side='right' caption='[[3ul5]], [[Resolution|resolution]] 2.30Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3ul5]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UL5 FirstGlance]. <br> | ||
| + | </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> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ul6|3ul6]]</td></tr> | ||
| + | <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 Saccharum officinarum])</td></tr> | ||
| + | <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://www.rcsb.org/pdb/explore.do?structureId=3ul5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ul5 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Saccharum officinarum]] | [[Category: Saccharum officinarum]] | ||
| - | [[Category: Garratt, R C | + | [[Category: Garratt, R C]] |
| - | [[Category: Oliveira-Silva, R | + | [[Category: Oliveira-Silva, R]] |
| - | [[Category: Pereira, H M | + | [[Category: Pereira, H M]] |
| - | [[Category: Valadares, N F | + | [[Category: Valadares, N F]] |
[[Category: Cystatin]] | [[Category: Cystatin]] | ||
[[Category: Defense]] | [[Category: Defense]] | ||
[[Category: Hydrolase inhibitor]] | [[Category: Hydrolase inhibitor]] | ||
Revision as of 07:00, 21 December 2014
Saccharum officinarum canecystatin-1 in space group C2221
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