2N1E

MAX1 peptide fibril

2N1E の概要

• エントリーDOI: 10.2210/pdb2n1e/pdb
• NMR情報: BMRB: 25558
• 分子名称: MAX1 peptide (1 entity in total)
• 機能のキーワード: designed peptide, hydrogel, biomaterials, amyloid-like, cross-beta, protein fibril
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 17895.78

構造登録者

Nagy-Smith, K.,Moore, E.,Schneider, J.,Tycko, R. (登録日: 2015-03-30, 公開日: 2015-07-29, 最終更新日: 2024-10-30)

主引用文献

Nagy-Smith, K.,Moore, E.,Schneider, J.,Tycko, R.
Molecular structure of monomorphic peptide fibrils within a kinetically trapped hydrogel network.
Proc.Natl.Acad.Sci.USA, 112:9816-9821, 2015

PubMed Abstract: Most, if not all, peptide- and protein-based hydrogels formed by self-assembly can be characterized as kinetically trapped 3D networks of fibrils. The propensity of disease-associated amyloid-forming peptides and proteins to assemble into polymorphic fibrils suggests that cross-β fibrils comprising hydrogels may also be polymorphic. We use solid-state NMR to determine the molecular and supramolecular structure of MAX1, a de novo designed gel-forming peptide, in its fibrillar state. We find that MAX1 adopts a β-hairpin conformation and self-assembles with high fidelity into a double-layered cross-β structure. Hairpins assemble with an in-register Syn orientation within each β-sheet layer and with an Anti orientation between layers. Surprisingly, although the MAX1 fibril network is kinetically trapped, solid-state NMR data show that fibrils within this network are monomorphic and most likely represent the thermodynamic ground state. Intermolecular interactions not available in alternative structural arrangements apparently dictate this monomorphic behavior.

PubMed: 26216960
DOI: 10.1073/pnas.1509313112

実験手法

SOLID-STATE NMR