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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 [alpha] 1
helix, the [alpha] 1/ [alpha] 2 loop and the [alpha] 3 helix with residues
from UBL from the [beta] 3, [beta] 4 and [beta] 5 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 [Goodford, P. J. (1985). J.
Med. Chem. 28, 849-858.]-[bluearr.gif] ) 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hydrophobic potential in grey (J. Gruber & M. E. M. Noble, unpublished work).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.
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