|
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.
|