6BXX

GYNGFG from low-complexity domain of hnRNPA1, residues 243-248

6BXX の概要

• エントリーDOI: 10.2210/pdb6bxx/pdb
• 分子名称: hnRNPA1 (2 entities in total)
• 機能のキーワード: amyloid, larks, reversible-amyloid, low-complexity, protein fibril
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 613.62

構造登録者

Hughes, M.P.,Rodriguez, J.A.,Sawaya, M.R.,Cascio, D.,Gonen, T.,Eisenberg, D.S. (登録日: 2017-12-19, 公開日: 2018-04-04, 最終更新日: 2024-03-13)

主引用文献

Hughes, M.P.,Sawaya, M.R.,Boyer, D.R.,Goldschmidt, L.,Rodriguez, J.A.,Cascio, D.,Chong, L.,Gonen, T.,Eisenberg, D.S.
Atomic structures of low-complexity protein segments reveal kinked beta sheets that assemble networks.
Science, 359:698-701, 2018

PubMed Abstract: Subcellular membraneless assemblies are a reinvigorated area of study in biology, with spirited scientific discussions on the forces between the low-complexity protein domains within these assemblies. To illuminate these forces, we determined the atomic structures of five segments from protein low-complexity domains associated with membraneless assemblies. Their common structural feature is the stacking of segments into kinked β sheets that pair into protofilaments. Unlike steric zippers of amyloid fibrils, the kinked sheets interact weakly through polar atoms and aromatic side chains. By computationally threading the human proteome on our kinked structures, we identified hundreds of low-complexity segments potentially capable of forming such interactions. These segments are found in proteins as diverse as RNA binders, nuclear pore proteins, and keratins, which are known to form networks and localize to membraneless assemblies.

PubMed: 29439243
DOI: 10.1126/science.aan6398

実験手法

X-RAY DIFFRACTION (1.1 Å)