Figure 6.
Comparison of the electrostatic surfaces of cUBA (A) and UBAb
(B). The orientation of both cUBA and UBAb is identical to that
of panels C and D in Figure 4 Figure 4.-.
The positive charges are shown in blue, and the negative charges
are colored in red. The surface presentation shows that the Ub
recognition surface on UBAb is predominately hydrophobic with
positively charged edges while the corresponding surface on cUBA
is something negatively charged in the center. The Ub
recognition surface on UBAb and its counterpart on cUBA are
highlighted by green parallelograms and labeled with amino acid
residues. The dimeric interfaces (indicated by green circles) of
cUBA (C) and UBAb (D) are rotated by [similar]180[deg] relative
to those in A and B, respectively. Residues I30 and I41 that are
involved in homodimerization are labeled. The PDB codes for the
structures are 2JUJ for cUBA and 2JNH for UBAb. (E) Glutamic
acid; (A) alanine; (I) isoleucine.
The above figure is reprinted
from an Open Access publication published by the Protein Society:
Protein Sci
(2008,
17,
1805-1814)
copyright 2008.
.
The positive charges are shown in blue, and the negative charges
are colored in red. The surface presentation shows that the Ub
recognition surface on UBAb is predominately hydrophobic with
positively charged edges while the corresponding surface on cUBA
is something negatively charged in the center. The Ub
recognition surface on UBAb and its counterpart on cUBA are
highlighted by green parallelograms and labeled with amino acid
residues. The dimeric interfaces (indicated by green circles) of
cUBA (C) and UBAb (D) are rotated by [similar]180[deg] relative
to those in A and B, respectively. Residues I30 and I41 that are
involved in homodimerization are labeled. The PDB codes for the
structures are 2JUJ for cUBA and 2JNH for UBAb. (E) Glutamic
acid; (A) alanine; (I) isoleucine.