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	Atomic structures of TDP-43 LCD segments and insights into reversible or pathogenic aggregation.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 25, Issue 6, Page 463-471, Year 2018
Publish date	May 21, 2018
Authors	Elizabeth L Guenther / Qin Cao / Hamilton Trinh / Jiahui Lu / Michael R Sawaya / Duilio Cascio / David R Boyer / Jose A Rodriguez / Michael P Hughes / David S Eisenberg /
PubMed Abstract	The normally soluble TAR DNA-binding protein 43 (TDP-43) is found aggregated both in reversible stress granules and in irreversible pathogenic amyloid. In TDP-43, the low-complexity domain (LCD) is ...The normally soluble TAR DNA-binding protein 43 (TDP-43) is found aggregated both in reversible stress granules and in irreversible pathogenic amyloid. In TDP-43, the low-complexity domain (LCD) is believed to be involved in both types of aggregation. To uncover the structural origins of these two modes of β-sheet-rich aggregation, we have determined ten structures of segments of the LCD of human TDP-43. Six of these segments form steric zippers characteristic of the spines of pathogenic amyloid fibrils; four others form LARKS, the labile amyloid-like interactions characteristic of protein hydrogels and proteins found in membraneless organelles, including stress granules. Supporting a hypothetical pathway from reversible to irreversible amyloid aggregation, we found that familial ALS variants of TDP-43 convert LARKS to irreversible aggregates. Our structures suggest how TDP-43 adopts both reversible and irreversible β-sheet aggregates and the role of mutation in the possible transition of reversible to irreversible pathogenic aggregation.
External links	Nat Struct Mol Biol / PubMed:29786080 / PubMed Central
Methods	EM (electron crystallography) / X-ray diffraction
Resolution	0.75 - 1.8 Å
Structure data	7466 6cf4 EMDB-7466, PDB-6cf4: Segment NFGTFS, with familial mutation A315T and phosphorylated threonine, from the low complexity domain of TDP-43, residues 312-317 Method: EM (electron crystallography) 7467 6cfh EMDB-7467: SWGMMGMLASQ segment from the low complexity domain of TDP-43, residues 333-343 PDB-6cfh: SWGMMGMLASQ segment from the low complexity domain of TDP-43 Method: EM (electron crystallography) 8857 5wkb EMDB-8857, PDB-5wkb: MicroED structure of the segment, NFGEFS, from the A315E familial variant of the low complexity domain of TDP-43, residues 312-317 Method: EM (electron crystallography) / Resolution: 1.0 Å PDB-5whn: Crystal structure of the segment, NFGAFS, from the low complexity domain of TDP-43, residues 312-317 Method: X-RAY DIFFRACTION / Resolution: 1.1 Å PDB-5whp: Crystal structure of the segment, NFGTFS, from the A315T familial variant of the low complexity domain of TDP-43, residues 312-317 Method: X-RAY DIFFRACTION / Resolution: 1.0 Å PDB-5wia: Crystal structure of the segment, GNNSYS, from the low complexity domain of TDP-43, residues 370-375 Method: X-RAY DIFFRACTION / Resolution: 1.002 Å PDB-5wiq: Crystal structure of the segment, GFNGGFG, from the low complexity domain of TDP-43, residues 396-402 Method: X-RAY DIFFRACTION / Resolution: 1.25 Å PDB-5wkd: Crystal structure of the segment, GNNQGSN, from the low complexity domain of TDP-43, residues 300-306 Method: X-RAY DIFFRACTION / Resolution: 1.8 Å PDB-6cb9: Segment AALQSS from the low complexity domain of TDP-43, residues 328-333 Method: X-RAY DIFFRACTION / Resolution: 1.1 Å PDB-6cew: Segment AMMAAA from the low complexity domain of TDP-43, residues 321-326 Method: X-RAY DIFFRACTION / Resolution: 1.2 Å
Chemicals	ChemComp-HOH: WATER / Water
Source	homo sapiens (human)
Keywords	PROTEIN FIBRIL / Amyloid / LARKS / TDP-43 / low complexity domain / Steric-zipper / Reversible aggregation / steric zipper