Figure 5
Contacts at the UBA–UBL interface. (a) Schematic representation of UBL (cyan) and UBA (green) showing the contact regions between UBA residues from the end of α1 helix, the α1/α2 loop and the α3 helix with residues from UBL from the β3, β4 and β5 strands. (b) Details of the contacts using the same colouring scheme as in (a). All residues from UBA and UBL that make contacts of <4.5 Å are shown. These are UBA residues D341, M342, G343, F344, Q362, L365, D366, L369 and G371 and UBL residues R43, I45, S47, G48, I50, H69, V71 and K72. The view is rotated ∼90° about the vertical axis from (a). (c) The van der Waals surface of UBL as seen by the UBA molecule with the UBA molecule and interacting residues superimposed. The hydrophobic potential (Goodford, 1985) of the surface is coloured with the deepest hydrophobicity yellow, the middle range in magenta and the surface with neutral hydrophobic potential in grey (J. Gruber & M. E. M. Noble, unpublished work). The surface has been made partially transparent to reveal the UBL structure and interacting residues. The UBL structure without the surface is shown on the right. The view is similar to (b) and 90° from (a). (d) A view 180° from (c) showing the van der Waals surface of UBA as seen by the UBL molecule, with the UBL molecule and interacting residues superimposed. The colouring is as in (c). The UBA molecule without the surface is shown on the right. |