Figure 2 - full size

 

Figure 2.
FIGURE 2. Molecular details of the UL44-UL54 interface. A, the connector loop of UL44 (white) and the UL54 peptide (brown) are joined by an extensive network of hydrogen bonds (green dots). Four intermolecular hydrogen bonds are formed between main chain atoms of the connector loop (residues 133-137) and the peptide (residues 1234-1238). Additional hydrogen bonds are observed between the side chain of Gln^133 (yellow) of UL44 and the main chain of the peptide and between the side chains of Gln^51 and Lys^60 (light blue) of UL44 and the main chain of the connector loop. Ile^135 (yellow) of UL44 forms a critical hydrophobic anchor below the hydrogen-bonding network. For clarity, only the side chains of Gln^51, Lys^60, Gln^133, and Ile^135 are shown. B, Leu^1227, Phe^1231, and Tyr^1234 (magenta) are part of a hydrophobic plug that packs against a hydrophobic crevice composed of Val^136 (yellow) from the connector loop (cyan) as well as hydrophobic and aliphatic side chains (green) from the central -sheet of UL44. C, the molecular surface of UL44 reveals pockets that accommodate the three-residue hydrophobic plug of UL54.

The above figure is reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 5224-5232) copyright 2006.