7N8R

FGTGFG segment from the Nucleoporin p54, residues 63-68

7N8R の概要

• エントリーDOI: 10.2210/pdb7n8r/pdb
• 分子名称: FGTGFG segment from the Nucleoporin p54, residues 63-68, trifluoroacetic acid (3 entities in total)
• 機能のキーワード: amyloid-like fibril, protein fibril
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 1283.27

構造登録者

Hughes, M.P.,Sawaya, M.R.,Eisenberg, D.S. (登録日: 2021-06-15, 公開日: 2022-02-16, 最終更新日: 2024-05-22)

主引用文献

Murray, K.A.,Evans, D.,Hughes, M.P.,Sawaya, M.R.,Hu, C.J.,Houk, K.N.,Eisenberg, D.
Extended beta-Strands Contribute to Reversible Amyloid Formation.
Acs Nano, 16:2154-2163, 2022

PubMed Abstract: The assembly of proteins into fibrillar amyloid structures was once considered to be pathologic and essentially irreversible. Recent studies reveal amyloid-like structures that form reversibly, derived from protein low-complexity domains which function in cellular metabolism. Here, by comparing atomic-level structures of reversible and irreversible amyloid fibrils, we find that the β-sheets of reversible fibrils are enriched in flattened (as opposed to pleated) β-sheets formed by stacking of extended β-strands. Quantum mechanical calculations show that glycine residues favor extended β-strands which may be stabilized by intraresidue interactions between the amide proton and the carbonyl oxygen, known as C5 hydrogen-bonds. Larger residue side chains favor shorter strands and pleated sheets. These findings highlight a structural element that may regulate reversible amyloid assembly.

PubMed: 35132852
DOI: 10.1021/acsnano.1c08043

実験手法

X-RAY DIFFRACTION (1.2 Å)