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. 2023 May 31;14:1192838. doi: 10.3389/fimmu.2023.1192838

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Copyright © 2023 Liu, Raab, Gui and Rudd

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The structure and binding sites of SKAP1. Human SKAP1 possesses an N-terminal dimerization (DM) domain, a species-specific disordered region, a pleckstrin homology (PH) domain (N107–K210), and a C-terminal SH3 domain (D294–E355) (33, 39). SKAP1 binds to ADAP via its SH3 domain and, to a lesser extent, via a SKAP1 RKxxYxxY motif that binds to an SH3C domain (41, 42). SKAP1 can form homodimers or heterodimers with related SKAP2 (SKAP-related R or SKAP-Hom) in cells mediated by residues A17 to L21 in the SKAP1 N-terminal region (43). The function of dimer formation is not known.