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Cryo electron microscopy of alpha-synuclein H50Q fibrils

ABSTRACT:

SUBMITTER: David R. Boyer

PROVIDER: EMPIAR-10632 | biostudies-other |

REPOSITORIES: biostudies-other

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Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs.

Boyer David R DR Li Binsen B Sun Chuanqi C Fan Weijia W Sawaya Michael R MR Jiang Lin L Eisenberg David S DS

Nature structural & molecular biology 20191106 11

Deposits of amyloid fibrils of α-synuclein are the histological hallmarks of Parkinson's disease, dementia with Lewy bodies and multiple system atrophy, with hereditary mutations in α-synuclein linked to the first two of these conditions. Seeing the changes to the structures of amyloid fibrils bearing these mutations may help to understand these diseases. To this end, we determined the cryo-EM structures of α-synuclein fibrils containing the H50Q hereditary mutation. We find that the H50Q mutati ...[more]

PMID: 31695184

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