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Figure 3.
Figure 3. The SAP25 SID binds to a deep hydrophobic cleft in
the mSin3A PAH1 domain. Molecular surface views of the cleft
color-coded according to (a) residue type (hydrophobic, yellow;
polar, cyan) and (b) curvature (concave, gray; planar, white;
convex, green). The backbone of the SAP25 SID helix and the
PAH1-interacting side-chains are shown in worm and in stick
representations, respectively. (c) A catalogue of intermolecular
interactions in the SAP25 SID–mSin3A PAH1 complex detected in
≥60% of conformers in the NMR ensemble.^64 SAP25 and mSin3A
residues are presented in pale magenta and pale green
backgrounds, respectively. The lines connect interacting
residues. Line colors indicate the type of interaction (green,
electrostatic; red, hydrogen bonding; purple, salt-bridge; gray,
hydrophobic), whereas text colors indicate the type of residue
(green, hydrophobic; blue, polar; magenta, charged).
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