Extended Data Fig. 6: Comparison of the structures of JIP1-SH3 and different variants.

a, Comparison of the crystal structures of JIP1-SH3(WT) (grey) and its V517L variant (green). The backbone conformation is entirely conserved with only minor rearrangements of protein side chains. b, Comparison of the crystal structures of the H493A (grey) and V517A (green) variants of JIP1-SH3. Structural features are conserved including similar side chain conformations. c, Comparison of the crystal structures of JIP1-SH3(WT) (grey) and its A541L variant (green) with arrows indicating the major conformational rearrangements between the WT protein and the variant. d, Illustration of the backbone conformation of the β-sheet formed between the 516–521 and 524–529 regions in the WT protein (left), and in the A541L variant (right). Dashed lines indicate hydrogen bonds. The A541L variant does not adopt a β-sheet conformation owing to the absence of several hydrogen bonds between the two β-strands. e, Schematic representation of the conformation of the β-strand encompassing residues 516 to 521 showing the orientation of the carbonyl group (“out” – carbonyl group surface exposed, “in” – carbonyl group pointing towards the β-strand encompassing residues 524 to 529) in the WT protein (left) and in the A541L variant (right). f, Volume of the Y526 pocket along the structural trajectory between the WT conformation and the conformations of the H493A/V517A mutants (grey) or A541L mutant (green). Conformations from the two structural trajectories at the maximum pocket volume are superimposed and shown in cartoon representation. The initial pocket expansion and its associated structural features are shared among all mutants.