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. 2020 May 12;7:89. doi: 10.3389/fmolb.2020.00089

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Copyright © 2020 Visconti, Toto, Jarvis, Troilo, Malagrinò, De Simone and Gianni.

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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Structural distribution of the residues (highlighted in red on N-SH2 structure) that are energetically coupled with M residue part of the pY-X-X-M consensus that is specifically recognized by N-SH2, and finely modulate the affinity of the domain for its natural binding partners (see text for details). Because of the unavailability of the N-SH2:Gab2 complex structure, a different ligand is represented in black (cKit) only to pinpoint the position of the binding pocket of N-SH2. (PDB: 2IUH).