Figure 5
Figure 5. ATLL FERM domain mutations align to the autoregulatory region of the FAK FERM based on homology modeling. ATLL mutations (orange) align with the F2 subdomain of the FAK FERM (blue) that autoregulates the kinase domain of FAK. Asterisks (*) denote residues of FAK FERM that contact the intramolecular FAK kinase domain. Molecular structure is based on the crystal structure of the FAK FERM domain. Those residues that are mutated in ATLL patients are highlighted (yellow). The JAK3 kinase domain (green) is shown as it would be oriented to the FERM domain. Below it, the respective kinase domains of FAK and JAK3 are aligned. The activation loop of the 2 proteins is in bold and the autoregulatory tyrosines, Y980 and Y981, are highlighted in orange. Asterisks (*) show the residues of FAK that contact the intramolecular FERM. The residues of JAK3 that align with these are shown in yellow.

ATLL FERM domain mutations align to the autoregulatory region of the FAK FERM based on homology modeling. ATLL mutations (orange) align with the F2 subdomain of the FAK FERM (blue) that autoregulates the kinase domain of FAK. Asterisks (*) denote residues of FAK FERM that contact the intramolecular FAK kinase domain. Molecular structure is based on the crystal structure of the FAK FERM domain. Those residues that are mutated in ATLL patients are highlighted (yellow). The JAK3 kinase domain (green) is shown as it would be oriented to the FERM domain. Below it, the respective kinase domains of FAK and JAK3 are aligned. The activation loop of the 2 proteins is in bold and the autoregulatory tyrosines, Y980 and Y981, are highlighted in orange. Asterisks (*) show the residues of FAK that contact the intramolecular FERM. The residues of JAK3 that align with these are shown in yellow.

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