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Figure 2.
Fig. 2. eRPTPµ dimerization. (A) Ribbon diagram of the
eRPTPµ dimer. The solvent-accessible surface is drawn in
light gray, and the domains appear in blue (MAM), magenta (Ig),
slate (FN1), yellow (FN2), green (FN3), and gray (FN4). The
asterisk marks the crystallographic twofold axis. (B)
Electrostatic properties. One monomer is shown as a
solvent-accessible surface colored by electrostatic potential
contoured at ±10 kT (red, acidic; blue, basic), and the
other monomer is shown as a black ribbon. (C) The dimer
interface. MAM and Ig domains of one molecule interact with FN1
and FN2 domains of another molecule. Domains are colored as in
(A). Residues involved in dimer interactions are drawn in stick
representation (oxygen, red; nitrogen, blue). Potential
hydrophilic interactions are marked as gray dotted lines.
Asterisks mark residues targeted for mutagenesis. (D)
Hydrophobic interactions. Color coding is as in (C), and the
N92-linked sugar is colored in green and forms stacking
interactions with the indole ring of W151. (E) Cell adhesion
assays. Non adherent insect Sf9 cells were infected with
baculovirus constructs expressing either enhanced green
fluorescent protein (EGFP) alone or RPTPµ-EGFP fusion
constructs, wild type and mutant, and observed by phase contrast
(top row) and fluorescence (bottom row) microscopy. Formation of
aggregates indicates RPTPµ ectodomain adhesive function
(8).
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