5w4i: Difference between revisions
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==X-ray crystallographic structure of a beta-hairpin peptide mimic derived from Abeta 16-36. Rigaku data set. (ORN)KLV(MEA)FAE(ORN)AIIGLMV.== | |||
<StructureSection load='5w4i' size='340' side='right'caption='[[5w4i]], [[Resolution|resolution]] 2.03Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5w4i]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W4I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W4I 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]] 2.026Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=MEA:N-METHYLPHENYLALANINE'>MEA</scene>, <scene name='pdbligand=ORN:L-ORNITHINE'>ORN</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=5w4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w4i OCA], [https://pdbe.org/5w4i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w4i RCSB], [https://www.ebi.ac.uk/pdbsum/5w4i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w4i ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The absence of high-resolution structures of amyloid oligomers constitutes a major gap in our understanding of amyloid diseases. A growing body of evidence indicates that oligomers of the beta-amyloid peptide Abeta are especially important in the progression of Alzheimer's disease. In many Abeta oligomers, the Abeta monomer components are thought to adopt a beta-hairpin conformation. This paper describes the design and study of a macrocyclic beta-hairpin peptide derived from Abeta16-36. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and size exclusion chromatography studies show that the Abeta16-36 beta-hairpin peptide assembles in solution to form hexamers, trimers, and dimers. X-ray crystallography reveals that the peptide assembles to form a hexamer in the crystal state and that the hexamer is composed of dimers and trimers. Lactate dehydrogenase release assays show that the oligomers formed by the Abeta16-36 beta-hairpin peptide are toxic toward neuronally derived SH-SY5Y cells. Replica-exchange molecular dynamics demonstrates that the hexamer can accommodate full-length Abeta. These findings expand our understanding of the structure, solution-phase behavior, and biological activity of Abeta oligomers and may offer insights into the molecular basis of Alzheimer's disease. | |||
A Hexamer of a Peptide Derived from Abeta16-36.,Kreutzer AG, Spencer RK, McKnelly KJ, Yoo S, Hamza IL, Salveson PJ, Nowick JS Biochemistry. 2017 Nov 14;56(45):6061-6071. doi: 10.1021/acs.biochem.7b00831., Epub 2017 Oct 27. PMID:29028351<ref>PMID:29028351</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5w4i" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Kreutzer AG]] | |||
[[Category: McKnelly KJ]] | |||
[[Category: Nowick JS]] | |||
Latest revision as of 09:43, 2 April 2025
X-ray crystallographic structure of a beta-hairpin peptide mimic derived from Abeta 16-36. Rigaku data set. (ORN)KLV(MEA)FAE(ORN)AIIGLMV.
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