Figure 3.
FIGURE 3. Comparison of local structures (at the mutation
site) between mutant and wild-type Fv-HEL complexes. a,
LY50A-HEL; b, HY33F-HEL; c, HY50F-HEL; d, HY58A-HEL; and e,
HY53A-HEL. C- atoms of all
polypeptide chains of each mutant complex are superimposed on
those of the wild-type complex. Wild-type complex is shown in
gray. Residues of VL, VH, and HEL of the mutant complexes are
shown in green, cyan, and pink, respectively. Water molecules
are shown as red balls. Hydrogen bonds in the mutant complexes
and wild-type complexes are depicted as red dotted lines and
gray dotted lines, respectively. The amino-aromatic (cation-
)
interaction is represented as a gray thick dashed line.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2007,
282,
6783-6791)
copyright 2007.
atoms of all
polypeptide chains of each mutant complex are superimposed on
those of the wild-type complex. Wild-type complex is shown in
gray. Residues of VL, VH, and HEL of the mutant complexes are
shown in green, cyan, and pink, respectively. Water molecules
are shown as red balls. Hydrogen bonds in the mutant complexes
and wild-type complexes are depicted as red dotted lines and
gray dotted lines, respectively. The amino-aromatic (cation-
)
interaction is represented as a gray thick dashed line.