PDBsum entry 2mj1

Hydrolase inhibitor

PDB id: 2mj1

Contents

Protein chain

18 a.a.

PDB id:

2mj1

Name:

Hydrolase inhibitor

Title:

Nmr structure of the soluble a beta 17-34 peptide

Structure:

Amyloid beta a4 protein. Chain: a. Fragment: unp residues 688-705. Synonym: abpp, appi, app, alzheimer disease amyloid protein, cerebral vascular amyloid peptide, cvap, prea4, protease nexin-ii, pn-ii, c83. Engineered: yes

Source:

Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606. Other_details: the peptide was chemically synthesized.

NMR struc:

11 models

Authors:

G.Fonar,A.O.Samson

Key ref:

G.Fonar and A.O.Samson (2014). NMR structure of the water soluble Aβ17-34 peptide. Biosci Rep, 34, e00155. PubMed id: 25284368 DOI: 10.1042/BSR20140094

Date:

23-Dec-13 Release date: 05-Nov-14

Protein chain

P05067  (A4_HUMAN) -  Amyloid-beta precursor protein from Homo sapiens

Seq: 770 a.a.

Struc: 18 a.a.

DOI no: 10.1042/BSR20140094

Biosci Rep 34:e00155 (2014)

PubMed id: 25284368

NMR structure of the water soluble Aβ17-34 peptide.

G.Fonar, A.O.Samson.

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.