Figure 3 - full size

 

Figure 3.
Figure 3 GW domains resemble SH3 domains. (A) Ribbon representation of GW and SH3 domains. Left: the Abl SH3 domain (blue), with bound peptide (green, backbone representation with prolines shown). The three peptide-binding pockets are numbered. Middle: InlB GW domain 2. Right: superposition of Abl SH3 (blue) and InlB GW (red), in C[ ]representation. (B) Structure-based sequence alignment of InlB GW domain 2, the L.monocytogenes p60 SH3b domain and the Abl SH3 domain. Residues responsible for peptide binding in the Abl SH3 domain are marked with numbers corresponding to binding pockets. Core residues conserved in GW and Abl are in blue, and secondary structure is indicated for GW domain 2 (top) and Abl (bottom). Gray shading marks the RT-loop, a red star indicates the intramolecular proline contact in InlB site 3, and a blue star indicates the substituted residue at InlB site 2. (C) Peptide-binding sites of Abl SH3 (blue, and bound peptide in green) and equivalent locations in InlB GW domains (red). (D) Molecular surface representations of the Abl SH3 domain and InlB GW domain 2. Numbers correspond to proline-binding sites (blue) in Abl and potential sites in the GW domain (blue). The RT-loop is colored red, and peptide bound to the SH3 domain is in green.

The above figure is reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2002, 21, 5623-5634) copyright 2002.