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Figure 2.
Interactions between the Efalizumab Fab and the LFA-1 α[L] I
domain. (A) A stereoview showing the interaction interface of
the Fab/I domain complex and the relative role of each CDR loop
in the interaction with the I domain. (B) An electrostatic
potential surface of the Fab at the interaction interface. There
are 2 negatively charged surface patches in the paratope to
accommodate several important residues of the I domain. Residues
of the I domain are shown side chains. The locations of some Fab
residues are indicated with white labels for references. (C) A
stereoview showing the hydrogen-bonding interactions between the
Fab heavy chain and the epitope of the I domain. The Fab
residues are colored in green and the I domain residues in
magenta. Hydrogen bonds are indicated by dashed lines. (D)
Sequence alignment of the I domains of all 9 known α
subunit-containing integrins in the region containing the
specificity determining residues. Residues corresponding to
Lys-197, Lys-200, and His-201 of the LFA-1 α[L] I domain are
indicated by blue boxes.
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