CryoEM of Tropomyosin-receptor kinase fused gene protein (TRK-fused gene protein; TFG) Low Complexity Domain (residues 237-327) G269V mutant, amyloid fibers
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ABSTRACT:
SUBMITTER: David Eisenberg
PROVIDER: EMPIAR-11929 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Fibril structures of TFG protein mutants validate the identification of TFG as a disease-related amyloid protein by the IMPAcT method.
Rosenberg Gregory M GM Abskharon Romany R Boyer David R DR Ge Peng P Sawaya Michael R MR Eisenberg David S DS
PNAS nexus 20231120 12
We previously presented a bioinformatic method for identifying diseases that arise from a mutation in a protein's low-complexity domain that drives the protein into pathogenic amyloid fibrils. One protein so identified was the tropomyosin-receptor kinase-fused gene protein (TRK-fused gene protein or TFG). Mutations in TFG are associated with degenerative neurological conditions. Here, we present experimental evidence that confirms our prediction that these conditions are amyloid-related. We find ...[more]
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