2OMP

LYQLEN peptide derived from human insulin chain A, residues 13-18

2OMP の概要

• エントリーDOI: 10.2210/pdb2omp/pdb
• 分子名称: LYQLEN peptide derived from human insulin chain A, residues 13-18 (2 entities in total)
• 機能のキーワード: steric zipper, antiparallel beta-sheet, protein fibril
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 1557.70

構造登録者

Ivanova, M.I.,Sawaya, M.R.,Eisenberg, D. (登録日: 2007-01-22, 公開日: 2007-01-30, 最終更新日: 2024-04-03)

主引用文献

Sawaya, M.R.,Sambashivan, S.,Nelson, R.,Ivanova, M.I.,Sievers, S.A.,Apostol, M.I.,Thompson, M.J.,Balbirnie, M.,Wiltzius, J.J.,McFarlane, H.T.,Madsen, A.O.,Riekel, C.,Eisenberg, D.
Atomic structures of amyloid cross-beta spines reveal varied steric zippers.
Nature, 447:453-457, 2007

PubMed Abstract: Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-beta spine. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. It is a pair of beta-sheets, with the facing side chains of the two sheets interdigitated in a dry 'steric zipper'. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. These include segments from the Alzheimer's amyloid-beta and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, alpha-synuclein and beta(2)-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.

PubMed: 17468747
DOI: 10.1038/nature05695

実験手法

X-RAY DIFFRACTION (1.9 Å)