Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular interactions of FG nucleoporin repeats at high resolution.
Journal, issue, pages	Nat Chem, Vol. 14, Issue 11, Page 1278-1285, Year 2022
Publish date	Sep 22, 2022
Authors	Alain Ibáñez de Opakua / James A Geraets / Benedikt Frieg / Christian Dienemann / Adriana Savastano / Marija Rankovic / Maria-Sol Cima-Omori / Gunnar F Schröder / Markus Zweckstetter /
PubMed Abstract	Proteins that contain repeat phenylalanine-glycine (FG) residues phase separate into oncogenic transcription factor condensates in malignant leukaemias, form the permeability barrier of the nuclear ...Proteins that contain repeat phenylalanine-glycine (FG) residues phase separate into oncogenic transcription factor condensates in malignant leukaemias, form the permeability barrier of the nuclear pore complex and mislocalize in neurodegenerative diseases. Insights into the molecular interactions of FG-repeat nucleoporins have, however, remained largely elusive. Using a combination of NMR spectroscopy and cryoelectron microscopy, we have identified uniformly spaced segments of transient β-structure and a stable preformed α-helix recognized by messenger RNA export factors in the FG-repeat domain of human nucleoporin 98 (Nup98). In addition, we have determined at high resolution the molecular organization of reversible FG-FG interactions in amyloid fibrils formed by a highly aggregation-prone segment in Nup98. We have further demonstrated that amyloid-like aggregates of the FG-repeat domain of Nup98 have low stability and are reversible. Our results provide critical insights into the molecular interactions underlying the self-association and phase separation of FG-repeat nucleoporins in physiological and pathological cell activities.
External links	Nat Chem / PubMed:36138110 / PubMed Central
Methods	EM (helical sym.)
Resolution	2.76 - 3.37 Å
Structure data	13851 7q64 EMDB-13851, PDB-7q64: Cryo-em structure of the Nup98 fibril polymorph 1 Method: EM (helical sym.) / Resolution: 2.76 Å 13852 7q65 EMDB-13852, PDB-7q65: Cryo-em structure of the Nup98 fibril polymorph 2 Method: EM (helical sym.) / Resolution: 3.32 Å 13853 7q66 EMDB-13853, PDB-7q66: Cryo-em structure of the Nup98 fibril polymorph 3 Method: EM (helical sym.) / Resolution: 2.79 Å 13854 7q67 EMDB-13854, PDB-7q67: Cryo-em structure of the Nup98 fibril polymorph 4 Method: EM (helical sym.) / Resolution: 3.37 Å
Source	homo sapiens (human)
Keywords	PROTEIN FIBRIL / Nuclear pore complex protein Nup98 functional amyloid fibril PROTEIN FIBRIL