Extended Data Fig. 7: Comparison of interfaces of p110γ-HD with GβγHD and p101-CTD with GβγCTD with those predicted by AlphaFold2. | Nature Structural & Molecular Biology

Extended Data Fig. 7: Comparison of interfaces of p110γ-HD with GβγHD and p101-CTD with GβγCTD with those predicted by AlphaFold2.

From: Molecular basis for Gβγ-mediated activation of phosphoinositide 3-kinase γ

Extended Data Fig. 7

(A) AlphaFold2 predicted residues on GβγHD (left panel) that interact with p110γ-HD (right panel). (B) AlphaFold2 predicted residues on GβγCTD (left panel) that interact with p101-CTD (right panel). (C) Experimentally determined interface residues on GβγHD (left panel) for interaction with p110γ-HD (right panel) in PI3Kγ·ADP–GβγHD. (D) Residues on GβγHD (left panel) involved in interaction with p110γ-HD (right panel) in state 1 of PI3Kγ·ADP–GβγHD–GβγCTD. (E) Residues on GβγCTD (left panel) that interact with p101-CTD (right panel) in PI3Kγ·ADP–GβγHD–GβγCTD. (F) Residues on GβγHD (left panel) that interact with p110γ-HD (right panel) in state 2 of PI3Kγ·ADP–GβγHD–GβγCTD. (G) Residues on GβγCTD (left panel) that interact with p101-CTD (right panel) in state 2 of PI3Kγ·ADP–GβγHD–GβγCTD.

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