Figure 1.
The diagram of the domain organization of human LCK and the positions of pathogenic variants. The diagram includes the SH4 and unique regions at the N-terminal for membrane localization, followed by the SH3 and SH2 domains for substrate binding, a linker region, the kinase domain, and a C-terminal tail. Key regulatory residues are indicated: Y192 and Y505 for inhibitory functions, Y394 for activating function, and K273 for engineered kinase-dead function. Reported human disease-associated variants are marked with red asterisks and mapped to their respective domains.
Domain organization of human LCK and positions of pathogenic variants. The schematic illustrates LCK structural domains: SH4 and unique regions (N-terminal membrane localization), SH3 and SH2 domains (substrate binding), linker region, kinase domain, and C-terminal tail. Key regulatory residues are indicated: Y192 and Y505 (inhibitory), Y394 (activating), and K273 (engineered kinase-dead). Reported human disease–associated variants (red asterisks) are mapped to their respective domains. SH, Src homology; Y, tyrosine; K, lysine.