5j0g
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P7/8== | |
| + | <StructureSection load='5j0g' size='340' side='right' caption='[[5j0g]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5j0g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J0G FirstGlance]. <br> | ||
| + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></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=5j0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j0g OCA], [http://pdbe.org/5j0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j0g RCSB], [http://www.ebi.ac.uk/pdbsum/5j0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j0g ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Despite continuing interest in partly unfolded proteins as precursors for aggregation and adverse gain-of-function in human disease, there is yet little known about the local transitions of native structures that possibly lead to such intermediate states. To target this problem, we present here a protein-design strategy that allows real-time detection of rupture and swapping of complete secondary-structure elements in globular proteins-molecular events that have previously been inaccessible experimental analysis. The approach is applied to the dynamic beta-barrel of SOD1, associated with pathologic aggregation in the neurodegenerative disease ALS. Data show that rupture and re-insertion of individual beta-strands do not take place locally but require the SOD1 barrel to unfold globally. The finding questions the very existence of partly unfolded intermediates in the SOD1 aggregation process and presents new clues to the mechanism by which hydrogen bonding maintains global structural integrity. | ||
| - | + | Tricking a Protein To Swap Strands.,Wang H, Lang L, Logan DT, Danielsson J, Oliveberg M J Am Chem Soc. 2016 Dec 7;138(48):15571-15579. Epub 2016 Nov 22. PMID:27783493<ref>PMID:27783493</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5j0g" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Superoxide dismutase]] | ||
[[Category: Danielsson, J]] | [[Category: Danielsson, J]] | ||
[[Category: Lang, L]] | [[Category: Lang, L]] | ||
| + | [[Category: Logan, D]] | ||
| + | [[Category: Oliveberg, M]] | ||
[[Category: Wang, H]] | [[Category: Wang, H]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Sod1]] | ||
Revision as of 18:01, 1 February 2017
Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, circular permutant P7/8
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