2MJ1

NMR structure of the soluble A beta 17-34 peptide

Summary for 2MJ1

• Entry DOI: 10.2210/pdb2mj1/pdb
• Related: 1LFM
• NMR Information: BMRB: 19701
• Descriptor: Amyloid beta A4 protein (1 entity in total)
• Functional Keywords: amyloid, alzheimer, hydrolase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P05067
• Total number of polymer chains: 1
• Total formula weight: 1851.13

Authors

Fonar, G.,Samson, A.O. (deposition date: 2013-12-23, release date: 2014-11-05, Last modification date: 2024-05-15)

Primary citation

Fonar, G.,Samson, A.O.
NMR structure of the water soluble A beta 17-34 peptide.
Biosci.Rep., 34:e00155-e00155, 2014

PubMed Abstract: Alzheimer's disease is the most common neurodegenerative disorder in the world. Its most significant symptoms are memory loss and decrease in cognition. Alzheimer's disease is characterized by aggregation of two proteins in the brain namely Aβ (amyloid β) and tau. Recent evidence suggests that the interaction of soluble Aβ with nAChR (nicotinic acetylcholine receptors) contributes to disease progression. In this study, we determine the NMR structure of an Aβ17-34 peptide solubilized by the addition of two glutamic acids at each terminus. Our results indicate that the Aβ peptide adopts an α-helical structure for residues 19-26 and 28-33. The α-helical structure is broken around residues S26, N27 and K28, which form a kink in the helical conformation. This α-helix was not described earlier in an aqueous solution without organic solvents, and at physiological conditions (pH 7). These data are in agreement with Aβ adopting an α-helical conformation in the membrane before polymerizing into amyloid β-sheets and provide insight into the intermediate state of Aβ in Alzheimer's disease.

PubMed: 25284368
DOI: 10.1042/BSR20140094

Experimental method

SOLUTION NMR