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. 2010 Mar 19;285(21):15906–15915. doi: 10.1074/jbc.M110.104349

FIGURE 4.

FIGURE 4.

Rational design of ICAM-1 D1 to convert surface-exposed hydrophobic residues into hydrophilic ones. A, shown are the histograms of the binding of anti-ICAM-1 mAb and the HA I domain to ICAM-1 D1.v2-containing I10R mutation. HA-Id, high affinity I domain. B, elution profiles are shown of D1.v2 containing I10R, I10T/P38R, I10R/P38T, and I10T/P38T from a Superdex-75 size exclusion column. mAU, milliabsorbance units. C, SPR measurement of the binding of the ICAM-1 D1.v3 to the HA I domain is shown. The analytes were injected in a series of 2-fold serial dilutions starting from 1 μm. RU, relative units. D, SDS-PAGE of induced (1) and uninduced (2) BL21 cell lysates and ICAM-1 D1.v3 after gel filtration column (3). E, schematic diagram of ICAM-1 D1 with modeled H-bond between Thr-38 and Ser-55 after P38T mutation.