View source for 8gjc


==X-ray crystallographic structure of a beta-hairpin peptide derived from Abeta 17-35. (ORN)LVFFAED(ORN)GAI(N-Me-Ile)GLM==
<StructureSection load='8gjc' size='340' side='right'caption='[[8gjc]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8gjc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GJC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GJC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.431&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IML:N-METHYL-ISOLEUCINE'>IML</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TFA:TRIFLUOROACETIC+ACID'>TFA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8gjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gjc OCA], [https://pdbe.org/8gjc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gjc RCSB], [https://www.ebi.ac.uk/pdbsum/8gjc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gjc ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Amyloid-beta (Abeta) forms heterogeneous oligomers, which are implicated in the pathogenesis of Alzheimer's disease (AD). Many Abeta oligomers consist of beta-hairpin building blocks horizontal line Abeta peptides in beta-hairpin conformations. beta-Hairpins of Abeta can adopt a variety of alignments, but the role that beta-hairpin alignment plays in the formation and heterogeneity of Abeta oligomers is poorly understood. To explore the effect of beta-hairpin alignment on the oligomerization of Abeta peptides, we designed and studied two model peptides with two different beta-hairpin alignments. Peptides Abetam(17-36) and Abetam(17-35) mimic two different beta-hairpins that Abeta can form, the Abeta(17-36) and Abeta(17-35) beta-hairpins, respectively. These hairpins are similar in composition but differ in hairpin alignment, altering the facial arrangements of the side chains of the residues that they contain. X-ray crystallography and SDS-PAGE demonstrate that the difference in facial arrangement between these peptides leads to distinct oligomer formation. In the crystal state, Abetam(17-36) forms triangular trimers that further assemble to form hexamers, while Abetam(17-35) forms tetrameric beta-barrels. In SDS-PAGE, Abetam(17-36) assembles to form a ladder of oligomers, while Abetam(17-35) either assembles to form a dimer or does not assemble at all. The differences in the behavior of Abetam(17-36) and Abetam(17-35) suggest beta-hairpin alignment as a source of the observed heterogeneity of Abeta oligomers.

beta-Hairpin Alignment Alters Oligomer Formation in Abeta-Derived Peptides.,Ruttenberg SM, Kreutzer AG, Truex NL, Nowick JS Biochemistry. 2024 Jan 16;63(2):212-218. doi: 10.1021/acs.biochem.3c00526. Epub , 2024 Jan 1. PMID:38163326<ref>PMID:38163326</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8gjc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Kreutzer AG]]
[[Category: Nowick JS]]
[[Category: Ruttenberg SM]]