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Figure 4.
Figure 4. A potential protein-protein binding interface of
UBA domains is built from hydrophobic residues on the surface.
(a) Surface representation of UBA(1) (left) using the following
color coding: red, acidic amino acid residues Glu and Asp; blue,
basic amino acid residues Arg and Lys, orange, polar amino acid
residues Asn, Gln, His, Ser and Thr; white, hydrophobic residues
Ala, Gly, Phe, Ile, Pro, Met, Leu, Tyr and Val. The major
accessible residues on the hydrophobic surface, Met173, Gly174,
Y175, L199 and I202, are marked. The size of the epitope is
approximately 470 Å2. The right picture shows the
orientation of the helical bundle with respect to the surface
representation. The hydrophobic surface patch consists mainly of
residues from loop 1 between helices 1 and 2 as well as residues
from helix 3. (b) For comparison, the surface of UBA(2) is shown
in the same orientation as UBA(1), revealing that the location
of the hydrophobic epitope is indeed conserved and consists of
identical or homologous residues. The C terminus of UBA(2) is
not shown, due to its flexibility.
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