Fig. 1. Molecular description of EhPAK. (A) The EhPAK region containing the few differences observed between the EhPAK (1) sequence (this paper) and the EhPAK (2) sequence (Gangopadhyay et al., 1997). (B) Amino-acid sequence comparison of EhPAK to the human PAK2 (HsPAK2). The N-terminal sequence of EhPAK shows a polybasic sequence (bold and italic) and a proline-rich sequence (italic) and the C-terminal sequence contains a predicted ATP-binding site (bold and underlined) and catalytic site (bold). The regulatory N-terminal sequence of human PAK2 contains the Nck-binding motif (bold), the polybasic region (italic), the CRIB domain (italic, bold and underlined) and the PIX interacting sequence (grey). The catalytic domain of HsPAK2 showing the ATP binding site (bold and underlined) and the catalytic site (bold). Accession numbers: EhPAK (1) EMBL X98048 and HsPAK2 (u24153.gb_pr). Sequence comparisons were performed with BESTFIT function in the GCG program. (C) Schematic representation of EhPAK and HsPAK2 showing their N-terminal region (oblique lines) and their catalytic domain (grey). The proline-rich sequence (open circle), CRIB motif (hatched box), ATP-binding site (black box) and catalytic site (white box) are indicated. (D) Shematic representation of the GST-hybrid fusion proteins produced in E. coli and purified.