1BJB

SOLUTION NMR STRUCTURE OF AMYLOID BETA[E16], RESIDUES 1-28, 14 STRUCTURES

1BJB の概要

• エントリーDOI: 10.2210/pdb1bjb/pdb
• 分子名称: AMYLOID BETA-PEPTIDE (1 entity in total)
• 機能のキーワード: glycoprotein, amyloid beta-peptide, alzheimer's disease
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P05067
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3268.44

構造登録者

Poulsen, S.-A.,Watson, A.A.,Craik, D.J. (登録日: 1998-06-23, 公開日: 1998-11-04, 最終更新日: 2024-05-22)

主引用文献

Poulsen, S.-A.,Watson, A.A.,Craik, D.J.
Solution structures in aqueous SDS micelles of two amyloid beta peptides of A beta(1-28) mutated at the alpha-secretase cleavage site (K16E, K16F)
J.Struct.Biol., 130:142-152, 2000

PubMed Abstract: NMRsolution structures are reported for two mutants (K16E, K16F) of the soluble amyloid beta peptide Abeta(1-28). The structural effects of these mutations of a positively charged residue to anionic and hydrophobic residues at the alpha-secretase cleavage site (Lys16-Leu17) were examined in the membrane-simulating solvent aqueous SDS micelles. Overall the three-dimensional structures were similar to that for the native Abeta(1-28) sequence in that they contained an unstructured N-terminus and a helical C-terminus. These structural elements are similar to those seen in the corresponding regions of full-length Abeta peptides Abeta(1-40) and Abeta(1-42), showing that the shorter peptides are valid model systems. The K16E mutation, which might be expected to stabilize the macrodipole of the helix, slightly increased the helix length (residues 13-24) relative to the K16F mutation, which shortened the helix to between residues 16 and 24. The observed sequence-dependent control over conformation in this region provides an insight into possible conformational switching roles of mutations in the amyloid precursor protein from which Abeta peptides are derived. In addition, if conformational transitions from helix to random coil to sheet precede aggregation of Abeta peptides in vivo, as they do in vitro, the conformation-inducing effects of mutations at Lys16 may also influence aggregation and fibril formation.

PubMed: 10940222
DOI: 10.1006/jsbi.2000.4267

実験手法

SOLUTION NMR