Fig. 1.

Overview of LD motifs. (A) Schematic representation of human paxillin family members (paxillin, leupaxin and Hic-5) and PaxB from Dictyostelium discoideum. TPR, tetratricopeptide repeat; Znf, zinc-finger; SAM, sterile α-motif; START, STAR-related lipid transfer domain. (B) Sequence alignment of selected known LD motifs. Sequence positions are numbered with respect to the first leucine of the LD motif (numbered 0). Acidic (red), basic (blue) and hydrophobic (green) residues are highlighted. PXN, paxillin. LPXN, leupaxin. All sequences are from human proteins, except for PaxB (D. discoideum). (C) Structure of LD motifs bound to FAK FAT and α-parvin. Ribbon diagrams of FAT and α-parvin are colour-ramped from blue (N-terminus) to red (C-terminus). LD motifs are shown in grey, with key residues shown as stick models in green (hydrophobic) or red (acidic). Position −1 (D), 0 (L) and +1 (E) are labelled