Fig. 1: PEAK domain organization and interaction motifs in N-terminal IDR. | Nature Communications

Fig. 1: PEAK domain organization and interaction motifs in N-terminal IDR.

From: Structural mapping of PEAK pseudokinase interactions identifies 14-3-3 as a molecular switch for PEAK3 signaling

Fig. 1

a Domain organization of the PEAK family and diagram of PEAK homodimer arrangement showing the SHED, PsK and IDR motifs identified (boxed). b Sequence alignment of the N-terminal IDR of human PEAK3 with the corresponding region of PEAK1 and PEAK2. c Multiple sequence alignment (MSA) of PEAK vertebrate orthologues highlighting short linear interaction motifs (SLiMs) identified in regions of high sequence conservation, including a pY/SH2 motif (Grb2SH2/CrkIISH2) and the tandem site encompassing a proline-rich motif (CrkIINSH3) and conserved putative 14-3-3 motif. d Schematic showing overall domain organization of Grb2, CrkII and 14-3-3, highlighting sequence motifs.

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