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-level evidence for packing and positional amyloid polymorphism by segment from TDP-43 RRM2.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 25, Issue 4, Page 311-319, Year 2018
Publish date	Mar 12, 2018
Authors	Elizabeth L Guenther / Peng Ge / Hamilton Trinh / Michael R Sawaya / Duilio Cascio / David R Boyer / Tamir Gonen / Z Hong Zhou / David S Eisenberg /
PubMed Abstract	Proteins in the fibrous amyloid state are a major hallmark of neurodegenerative disease. Understanding the multiple conformations, or polymorphs, of amyloid proteins at the molecular level is a ...Proteins in the fibrous amyloid state are a major hallmark of neurodegenerative disease. Understanding the multiple conformations, or polymorphs, of amyloid proteins at the molecular level is a challenge of amyloid research. Here, we detail the wide range of polymorphs formed by a segment of human TAR DNA-binding protein 43 (TDP-43) as a model for the polymorphic capabilities of pathological amyloid aggregation. Using X-ray diffraction, microelectron diffraction (MicroED) and single-particle cryo-EM, we show that the DLIIKGISVHI segment from the second RNA-recognition motif (RRM2) forms an array of amyloid polymorphs. These associations include seven distinct interfaces displaying five different symmetry classes of steric zippers. Additionally, we find that this segment can adopt three different backbone conformations that contribute to its polymorphic capabilities. The polymorphic nature of this segment illustrates at the molecular level how amyloid proteins can form diverse fibril structures.
External links	Nat Struct Mol Biol / PubMed:29531287 / PubMed Central
Methods	EM (electron crystallography) / EM (helical sym.) / X-ray diffraction
Resolution	1.4 - 3.8 Å
Structure data	8765 5w52 EMDB-8765, PDB-5w52: MicroED structure of the segment, DLIIKGISVHI, from the RRM2 of TDP-43, residues 247-257 Method: EM (electron crystallography) 8781 5w7v EMDB-8781, PDB-5w7v: CryoEM structure of the segment, DLIIKGISVHI, assembled into a triple-helical fibril Method: EM (helical sym.) / Resolution: 3.8 Å PDB-5w50: Crystal structure of the segment, LIIKGI, from the RRM2 of TDP-43, residues 248-253 Method: X-RAY DIFFRACTION / Resolution: 1.4 Å
Chemicals	ChemComp-HOH: WATER / Water
Source	homo sapiens (human)
Keywords	PROTEIN FIBRIL / Amyloid / steric zipper