5V63

Crystal structure of macrocycles containing Abeta 16-22 (KLV(PHI)FAE) and Abeta 30-36 (AII(SAR)L(ORN)V)

Summary for 5V63

• Entry DOI: 10.2210/pdb5v63/pdb
• Related: 5V64 5V65
• Descriptor: ORN-LYS-LEU-VAL-PHI-PHE-ALA-GLU-ORN-ALA-ILE-ILE-SAR-LEU-MET-VAL (2 entities in total)
• Functional Keywords: beta-hairpin, macrocycle, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 2019.30

Authors

Spencer, R.K.,Salveson, P.J.,Nowick, J.S. (deposition date: 2017-03-15, release date: 2017-06-28, Last modification date: 2020-01-01)

Primary citation

Salveson, P.J.,Spencer, R.K.,Kreutzer, A.G.,Nowick, J.S.
X-ray Crystallographic Structure of a Compact Dodecamer from a Peptide Derived from A beta 16-36.
Org. Lett., 19:3462-3465, 2017

PubMed Abstract: The assembly of the β-amyloid peptide, Aβ, into soluble oligomers is associated with neurodegeneration in Alzheimer's disease. The Aβ oligomers are thought to be composed of β-hairpins. Here, the effect of shifting the residue pairing of the β-hairpins on the structures of the oligomers that form is explored through X-ray crystallography. Three residue pairings were investigated using constrained macrocyclic β-hairpins in which Aβ is juxtaposed with Aβ, Aβ, and Aβ. The Aβ-Aβ 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 Aβ.

PubMed: 28683555
DOI: 10.1021/acs.orglett.7b01445

Experimental method

X-RAY DIFFRACTION (2.091 Å)