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. 2020 Mar 6;3:109. doi: 10.1038/s42003-020-0831-6

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© This is a U.S. government work and not under copyright protection in the U.S.; foreign copyright protection may apply 2020

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Fig. 4 — a Synaptamide binding pocket located in the interface of the two subdomains. The protein surface is colored with hydrophobicity (blue, polar; yellow-gray, hydrophobic). b Amino acid residues predicted to interact with synaptamide. c The inter-subdomain cross-linking of K398-K438 detected by in-cell cross-linking and mass spectrometry. Subdomains A and B are colored with magenta and cyan respectively. Among eight cross-linked lysine pairs observed, only the cross-link of K398-K438 (depicted by dotted line) changed after synaptamide binding. Lysin residues (stick representation) involving in the cross-linking reactions were labeled. The GAIN domain (AA 251–580) was modeled using the crystal structure of BAI3 (pdb 4DLO) as a template. Synaptamide is shown with a space-filling (a, c) or stick and ball representation (b).