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Figure 4.
Figure 4. (a) Structure-based sequence alignment of the SH3
domains of PLCg1, PLCg2 and Lck. Secondary structure elements
are denoted by violet arrows (b-strands) and a pink cylinder
(3[10] helix). These, and the loop regions (brown lines), are
labeled according to the nomenclature for Src-SH3.22 Residues of
PLCg1-SH3 making van der Waals contacts with SLP-76 are shaded
yellow; residues interacting with SLP-76 through hydrogen bonds
are shaded cyan. Asp808, which forms a salt-bridge with the
bound peptide, is shaded red. (b) Superposition of PLCg1-SH3 in
bound form (cyan) onto free Lck-SH3 (green; PDB accession code
1LCK).28 The view is the same as that in Figure 3(c). Residues
of Lck-SH3 that potentially contact bound peptide, based on
sequence alignment with PLCg1-SH3 (a), are shown. (c)
Interactions at the SH3 compass pocket. The PLCg1/SLP-76 complex
(cyan) was superposed onto the Src-SH3/App12 complex (PDB
accession code 1QWE)30 and free Lck-SH3. Only interactions with
the compass residue of the bound peptide (Arg192 of SLP-76 and
Arg9 of App12) are shown. Salt-bridges are drawn as broken lines.
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