5v64: Difference between revisions

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'''Unreleased structure'''


The entry 5v64 is ON HOLD  until Paper Publication
==Crystal structure of macrocycles containing Abeta 15-21 (QKLV(PHI)FA) and Abeta 30-36 (AII(SAR)L(ORN)V)==
<StructureSection load='5v64' size='340' side='right' caption='[[5v64]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5v64]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V64 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V64 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene>, <scene name='pdbligand=PHI:IODO-PHENYLALANINE'>PHI</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v65|5v65]], [[5v63|5v63]]</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=5v64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v64 OCA], [http://pdbe.org/5v64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v64 RCSB], [http://www.ebi.ac.uk/pdbsum/5v64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v64 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The assembly of the beta-amyloid peptide, Abeta, into soluble oligomers is associated with neurodegeneration in Alzheimer's disease. The Abeta oligomers are thought to be composed of beta-hairpins. Here, the effect of shifting the residue pairing of the beta-hairpins on the structures of the oligomers that form is explored through X-ray crystallography. Three residue pairings were investigated using constrained macrocyclic beta-hairpins in which Abeta30-36 is juxtaposed with Abeta17-23, Abeta16-22, and Abeta15-21. The Abeta16-22-Abeta30-36 pairing forms a compact ball-shaped dodecamer composed of fused triangular trimers. This dodecamer may help explain the structures of the trimers and dodecamers formed by full-length Abeta.


Authors:  
X-ray Crystallographic Structure of a Compact Dodecamer from a Peptide Derived from Abeta16-36.,Salveson PJ, Spencer RK, Kreutzer AG, Nowick JS Org Lett. 2017 Jul 7;19(13):3462-3465. doi: 10.1021/acs.orglett.7b01445. Epub, 2017 Jun 15. PMID:28683555<ref>PMID:28683555</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5v64" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Nowick, J S]]
[[Category: Salveson, P J]]
[[Category: Spencer, R K]]
[[Category: Beta-hairpin]]
[[Category: De novo protein]]
[[Category: Macrocycle]]
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