5v65

Crystal structure of macrocycles containing Abeta 17-23 (LV(PHI)FAED) and Abeta 30-36 (AII(SAR)L(ORN)V)

spinqualitylabelsall models 5v65, resolution 2.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5v65 is a 16 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.52Å Ligands: ORN, PHI, SAR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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