Figure 7
Figure 7. Comparison of 14-3-3–binding peptides and integrins. (A) Alignment of mode 1 and mode 2 14-3-3–binding consensus sequences with integrin sequences. (B) Superimposition of our 14-3-3 bound β2 (orange) with mode 1 (PDB entry 1QJB, purple) and mode 2 (PDB entry 1QJA, yellow) peptide structures. The only common features are the Arg/Lys and the pThr/pSer indicated in red in panel A. (C) Superimposition of β2 peptides in 14-3-3–binding conformation (orange) and IgFLNa21-binding conformation (green) shows that in both complexes the peptides are extended, but the side chain orientations differ markedly. (D) Sequence alignment of talin-, filamin-, and 14-3-3–binding sites in different integrin β-chains. The binding sites are based on the β3-talin complex structure 1MIZ21 and our current structures (β2/14-3-3 and β2/filamin).

Comparison of 14-3-3–binding peptides and integrins. (A) Alignment of mode 1 and mode 2 14-3-3–binding consensus sequences with integrin sequences. (B) Superimposition of our 14-3-3 bound β2 (orange) with mode 1 (PDB entry 1QJB, purple) and mode 2 (PDB entry 1QJA, yellow) peptide structures. The only common features are the Arg/Lys and the pThr/pSer indicated in red in panel A. (C) Superimposition of β2 peptides in 14-3-3–binding conformation (orange) and IgFLNa21-binding conformation (green) shows that in both complexes the peptides are extended, but the side chain orientations differ markedly. (D) Sequence alignment of talin-, filamin-, and 14-3-3–binding sites in different integrin β-chains. The binding sites are based on the β3-talin complex structure 1MIZ21  and our current structures (β2/14-3-3 and β2/filamin).

Close Modal

or Create an Account

Close Modal
Close Modal