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Figure 3.
Figure 3. Protein–Protein Interactions in On TEBP(A)
Surface representation of the protein–protein association. α
is shown as a solvent-accessible surfaceβ is shown as an
α-carbon trace in blue, and the ssDNA is shown as a ribbon with
boxes for the base groups (yellow, G; blue, T). A large groove
that associates with helix C[β] of β is apparent, as are the
surfaces that interact with the extended peptide loop of β. Two
leucine residues at the surface of α that interact with the
N-terminal portion of helix C[β] are indicated by the colored
patches on α, with purple showing the location of L236[α] and
green showing the location of L330[α]. Three residues at the
C-terminal region of helix C[β] form a hydrophobic ridge, and
these are shown in blue. From the middle of helix C[β] to the
C-terminal end these residues are L156[β], I160[β], and
V164[β].(B) Detailed view of the residues at the
protein–protein interface. Notice how helix C[β] of β (blue)
bridges the N-terminal (purple) and C-terminal (green) domains
of α. The peptide loop of β follows directly after the last
turn of this helix (residue V164[β]). Hydrophobic side chains
(gray) close to the surface of the α C-terminal domain create
two hydrophobic patches that align with clusters of hydrophobic
residues located along this extended peptide loop of β.
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