Fig. 5: Modelling the Las17-actin interactions through global docking.

All residues are shown as a cartoon ribbon except for arginines that flank the polyproline sequence of the ABS sites, and key interacting actin residues. Yeast G-actin is shown in green (PDB: 1YAG). A Structures for four of the top ten HPEPDOCK predictions of ABS3 docking show interactions in the barbed end groove of the actin monomer. Peptides are shown in different colours. B All four of these structures coordinate actin residue E334 via the double arginine pair (R6 and R7 in the docked peptide). C A structure illustrating one of the top ten structure predictions for ABS1 shows how arginines at each end of the peptide of Las17 may interact simultaneously with acidic residues flanking the barbed end groove of actin (E334, and E361/364). D All three docked peptide structures can be modelled to illustrate binding of three actin monomers along the Las17 peptide. The ABS sequences are shown in red whilst the adjoining sequences that were part of the modelling in pink. The dashed pink line indicates parts of Las17 with no structural information.