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Fig. 1 | Cell Communication and Signaling

Fig. 1

From: Experimental detection of short regulatory motifs in eukaryotic proteins: tips for good practice as well as for bad

Fig. 1

Linear motifs in T cell signalling complex assembly. Four structures of SLiM-domain complexes are combined to show the involvement of motifs in assembly of the T cell receptor signalling complex around the adaptor molecule Linker for activation of T-cells family member 1 (LAT). A phosphorylated SH2 domain-binding motif (YxN) in LAT (189-REYVNV-194, shown in dark blue with the phosphorylated Y191 in red) recruits GRB2-related adapter protein 2 (GADS) via its SH2 domain (grey) (bottom left) (PDB:1R1Q) [79], while the C-terminal SH3 domain of GADS (grey) binds an SH3 domain-binding motif in Lymphocyte cytosolic protein 2 (SLP-76) (233-PSIDRSTKP-241, shown in green) (bottom right) (PDB:2D0N) [80]. Further components are recruited to the complex through other motifs in SLP-76, including an SH3 domain-binding motif (185-QPPVPPQRPM-194, shown in green) that interacts with the SH3 domain of 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (PLCG1) (purple) (top right) (PDB:1YWO) [81], and an SH2 domain-binding motif (143-ADYEPP-148, shown in green with the phosphorylated Y145 in red) binding to the SH2 domain of Tyrosine-protein kinase ITK/TSK (ITK) (light blue) (top left) (PDB:2ETZ) [82]

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