5lfy
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Zinc bound dimer of the fragment of human amyloid-beta peptide with Alzheimer's disease pathogenic Taiwanese mutation D7H== | |
| + | <StructureSection load='5lfy' size='340' side='right' caption='[[5lfy]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lfy]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LFY FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=5lfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfy OCA], [http://pdbe.org/5lfy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lfy RCSB], [http://www.ebi.ac.uk/pdbsum/5lfy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Zinc-induced oligomerization of amyloid-beta peptide (Abeta) produces potentially pathogenic agents of Alzheimer's disease. Mutations and modifications in the metal binding domain 1-16 of Abeta peptide crucially affect its zinc-induced oligomerization by changing intermolecular zinc mediated interface. The 3D structure of this interface appearing in a range of Abeta species is a prospective drug target for disease modifying therapy. Using NMR spectroscopy, EXAFS spectroscopy, mass spectrometry, and isothermal titration calorimetry the interaction of zinc ions with Abeta fragments 1-7 and 1-10 carrying familial Taiwanese mutation D7H was studied. Zinc ions induce formation of a stable homodimer formed by the two peptide chains fastened by two zinc ions and stacking interactions of imidazole rings. A binuclear zinc interaction fold in the dimer structure was discovered. It can be used for designing zinc-regulated proteins and zinc-mediated self-assembling peptides. | ||
| - | + | A Binuclear Zinc Interaction Fold Discovered in the Homodimer of Alzheimer's Amyloid-beta Fragment with Taiwanese Mutation D7H.,Polshakov VI, Mantsyzov AB, Kozin SA, Adzhubei AA, Zhokhov SS, van Beek W, Kulikova AA, Indeykina MI, Mitkevich VA, Makarov AA Angew Chem Int Ed Engl. 2017 Jun 1. doi: 10.1002/anie.201704615. PMID:28570778<ref>PMID:28570778</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Mantsyzov, A | + | <div class="pdbe-citations 5lfy" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kozin, S A]] | ||
| + | [[Category: Mantsyzov, A B]] | ||
| + | [[Category: Polshakov, V I]] | ||
| + | [[Category: Alzheimer's disease]] | ||
| + | [[Category: Amyloid-beta peptide]] | ||
| + | [[Category: Structural protein]] | ||
| + | [[Category: Zinc complex]] | ||
| + | [[Category: Zinc-bound dimer]] | ||
Revision as of 11:10, 24 August 2017
Zinc bound dimer of the fragment of human amyloid-beta peptide with Alzheimer's disease pathogenic Taiwanese mutation D7H
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