Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2 Highlights d KIR3DL1 cytoplasmic domain is intrinsically disordered with three distinct segments d TFE and SDS enhanced a-helical conformation around the two tyrosines (ITIMs) d SHP-2 SH2 domains decrease NMR peaks around the unphosphorylated N-terminal ITIM d Bis-phosphorylated ITIMs are more broadly impacted by the tandem SHP-2 SH2 domains
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