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Figure 3.
Figure 3. Solution Structure of ItchWW3 in Complex with the
PY Peptide—1′-EEPPPPYED-9′
(A) Stereo view of the
best-fit backbone (N, C^α, C′) superposition of the ten
lowest-energy structures after water refinement. The backbone is
shown in blue, with selected side chains represented in magenta
(domain) and green (peptide). Some selected residues are
labeled. Residue numbers are maintained as in the reference
(Shaw et al., 2005). L6 corresponds to L401 in the full protein
sequence. In the peptide, the conversion is such that E2′
corresponds to E55.
(B) Lowest-energy structure of the
complex with the domain shown as a solid surface representation
(in gold) and with the same orientation as above. The peptide is
shown by blue lines. Residues located in the binding site as
well as both tyrosine and proline binding grooves are labeled.
The green circle displays additional contacts observed in the
complex.
(C) Surface electrostatic representation of the
complex rotated by 90° around the x axis with respect to the
orientation shown in (B). The left green circle displays the
electrostatic complementation observed between the aspartic acid
D9′ in the peptide and both H25 and R13 in the domain. This
interaction is supported by NOEs from the peptide to the domain.
The right circle displays the potential contacts between
arginine 19 in the domain and E2′ in the peptide.
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