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- W2802005789 abstract "Abstract Epilepsy is a common brain disorder throughout history. Epilepsy-related ligand–receptor complex, LGI1–ADAM22, regulates synaptic transmission and has emerged as a determinant of brain excitability, as their mutations and acquired LGI1 autoantibodies cause epileptic disorders in human. Here, we report the crystal structure of human LGI1–ADAM22 complex, revealing a 2:2 heterotetrameric assembly. The hydrophobic pocket of the C-terminal epitempin-repeat (EPTP) domain of LGI1 binds to the metalloprotease-like domain of ADAM22. The N-terminal leucine-rich repeat and EPTP domains of LGI1 mediate the intermolecular LGI1–LGI1 interaction. A pathogenic R474Q mutation of LGI1, which does not exceptionally affect either the secretion or the ADAM22 binding, is located in the LGI1–LGI1 interface and disrupts the higher-order assembly of the LGI1–ADAM22 complex in vitro and in a mouse model for familial epilepsy. These studies support the notion that the LGI1–ADAM22 complex functions as the trans-synaptic machinery for precise synaptic transmission." @default.
- W2802005789 created "2018-05-17" @default.
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- W2802005789 date "2018-04-18" @default.
- W2802005789 modified "2023-10-14" @default.
- W2802005789 title "Structural basis of epilepsy-related ligand–receptor complex LGI1–ADAM22" @default.
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- W2802005789 doi "https://doi.org/10.1038/s41467-018-03947-w" @default.
- W2802005789 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5906670" @default.
- W2802005789 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29670100" @default.
- W2802005789 hasPublicationYear "2018" @default.
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