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• W2128984988 abstract "The aggregation of acetylcholine receptors on postsynaptic membranes is a key step in neuromuscular junction development. This process depends on alternatively spliced forms of the proteoglycan agrin with “B-inserts” of 8, 11, or 19 residues in the protein's globular C-terminal domain, G3. Structures of the neural B8 and B11 forms of agrin-G3 were determined by X-ray crystallography. The structure of G3-B0, which lacks inserts, was determined by NMR. The agrin-G3 domain adopts a β jellyroll fold. The B insert site is flanked by four loops on one edge of the β sandwich. The loops form a surface that corresponds to a versatile interaction interface in the family of structurally related LNS proteins. NMR and X-ray data indicate that this interaction interface is flexible in agrin-G3 and that flexibility is reduced by Ca2+ binding. The plasticity of the interaction interface could enable different splice forms of agrin to select between multiple binding partners." @default.
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• W2128984988 date "2004-03-01" @default.
• W2128984988 modified "2023-10-16" @default.
• W2128984988 title "Modulation of Agrin Function by Alternative Splicing and Ca2+ Binding" @default.
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• W2128984988 doi "https://doi.org/10.1016/j.str.2004.02.001" @default.
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