Figure 1

Structure of RACK1 proteins. (A) Sequence alignment of RACK1 orthologues and their UniProt accession numbers from H. sapiens (P63244), D. melanogaster (O18640), A. thaliana (O24456), D. discoideum (DdRACK1) (P46800) and S. cerevisiae (P38011). The WD40 repeats and β-propeller blade positions are written above the sequences. Alignment was done with the ClustalW program and processed through ESPript for representation. All conserved residues are shown in red and similar residues in yellow. (B) Ribbon diagram of S. cerevisiae RACK1 (Asc1p) (PDB: 3FRX) which was used as template for DdRACK1 model. Shown are the seven β-propeller blades. Coordinates were retrieved from protein data bank (PDB) (http://www.rcsb.org) and modelled with the aid of MODELLER v9 program and visualized by the software PyMOL. (C) Ribbon structure of DdRACK1 (DDB0185122) showing (a), the side view of the β-propeller blades with some of the residues in the extended loop between blades 6 and 7 shown in ball and stick model, (b) the top view of the β-propeller blades with the same extended loop as in (a), and (c) the surface properties of DdRACK1 (WT) and DdRACK1mut (mut). Arrowheads pointing to blue and red regions indicate non-mutated and mutated residues, respectively. Structures were modeled and generated with the aid of MODELLER v9 program and visualized using molecular visualization software PyMOL.