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Sequence alignment of PHCCEx domains with secondary structure elements of the Tiam2 PHCCEx domain at the top. Sequence alignment of PHCCEx domains with.

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Presentation on theme: "Sequence alignment of PHCCEx domains with secondary structure elements of the Tiam2 PHCCEx domain at the top. Sequence alignment of PHCCEx domains with."— Presentation transcript:

1 Sequence alignment of PHCCEx domains with secondary structure elements of the Tiam2 PHCCEx domain at the top. Sequence alignment of PHCCEx domains with secondary structure elements of the Tiam2 PHCCEx domain at the top. Conserved and semi‐invariant (E=D, R=K=H, T=S, F=Y, V=L=I=M=C) residues are highlighted in yellow and blue‐green, respectively. Acidic and basic residues are in red and blue, respectively. Residues predicted to be involved in interactions with phosphoinositides are indicated by red circles. Residues that were shown to be important for CD44 binding are indicated by blue circles. The Tiam1 missense mutation is indicated by a box. Shin‐ichi Terawaki et al. EMBO J. 2010;29: © as stated in the article, figure or figure legend

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