Figure 5.
Figure 5. Amino acid sequence alignment of the ATP-binding site region of human JAK2 PTK domain with the other members of the JAK family TYK2, JAK3, and JAK1 and the kinase domain of FAK, IRK, ZAP-70, FGFR2, and LCK. The secondary structure of JAK2 is illustrated directly above the sequence alignment. Arrows delineate β-strands, and cylinders delineate α-helices. Dark gray boxes indicate conserved residues; light gray boxes, conservatively substituted residues. Residues highlighted in blue are located in the adenine-binding region; in green, in the sugar pocket; and in pink, in the phosphate-binding region. Residues accessible to solvent are colored in brown and buried residues are colored in purple. IC50s of CMP6 for each kinase are indicated on the right.

Amino acid sequence alignment of the ATP-binding site region of human JAK2 PTK domain with the other members of the JAK family TYK2, JAK3, and JAK1 and the kinase domain of FAK, IRK, ZAP-70, FGFR2, and LCK. The secondary structure of JAK2 is illustrated directly above the sequence alignment. Arrows delineate β-strands, and cylinders delineate α-helices. Dark gray boxes indicate conserved residues; light gray boxes, conservatively substituted residues. Residues highlighted in blue are located in the adenine-binding region; in green, in the sugar pocket; and in pink, in the phosphate-binding region. Residues accessible to solvent are colored in brown and buried residues are colored in purple. IC50s of CMP6 for each kinase are indicated on the right.

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