Results: 4

1.
FIGURE 4

FIGURE 4. From: Role of the β-Subunit Arginine/Lysine Finger in Integrin Heterodimer Formation and Function.

Effect of K252A and K252R on ligand binding. Left, Histograms showing the binding of the physiologic ligand iC3b or the ligand mimic 107 to mutant CD11b/CD18 relative to that of WT (placed at 100), after correcting for receptor expression using mAb TS1/18. Each histogram represents mean ± SD of triplicate (for iC3b) or quadruplet (for 107) determinations from a representative experiment (of three performed). Details of the methods used are described in Materials and Methods.

Vineet Gupta, et al. J Immunol. ;180(3):1713-1718.
2.
FIGURE 3

FIGURE 3. From: Role of the β-Subunit Arginine/Lysine Finger in Integrin Heterodimer Formation and Function.

Effect of Arg/Lys mutations on surface expression and formation of integrin CD11b/CD18. A, Surface expression of WT and mutant CD11b/CD18. Histograms (mean ± SD of triplicate determinations from a representative experiment, one of three performed) showing expression levels of WT and mutant CD11b/CD18 receptors in transfected HEK 293 cells. Surface expression was evaluated with the anti-CD11b mAbs 903 and 44a and the anti-CD18 mAbs TS1/18 mAbs. B, Western blots following 4 –15% gradient SDS-PAGE developed with polyclonal anti-CD11b (upper and lower) or anti-CD18 Abs (middle) of whole cell lysate from HEK 293 cells expressing WT or mutant receptors (upper and middle) or anti-CD18 mAb immunoprecipitates probed with polyclonal anti-CD11b Ab (lower) (one representative experiment is shown of three conducted).

Vineet Gupta, et al. J Immunol. ;180(3):1713-1718.
3.
FIGURE 2

FIGURE 2. From: Role of the β-Subunit Arginine/Lysine Finger in Integrin Heterodimer Formation and Function.

Effect of R261A and R261E on surface expression and αVβ3 heterodimer formation. In this and subsequent figures, amino acids are indicated in the single letter code. A, Histograms showing expression of recombinant WT and mutant αVβ3 on the cell surface of transfected HEK293 cells, probed with the anti-αV mAb LM142, the anti-β3 mAb AP3 or the heterodimer specific mAb LM609. Each histogram represents mean ± SD of triplicate determinations from three independent experiments. B, Western blots, following 4–15% gradient SDS-PAGE, developed with polyclonal anti-αV Ab (upper and lower,) and anti-β3 CBL479 mAb (middle). Equivalent amounts of βV- (upper) and WT or mutant β3-subunits (middle) are detected. Immunoprecipitation with anti-β3 mAb AP3 from HEK 293 cells expressing WT or mutant receptors revealed much reduced levels of the associated αV-subunit in the R261E mutant, compared with WT or R216A receptors (one representative experiment of four conducted).

Vineet Gupta, et al. J Immunol. ;180(3):1713-1718.
4.
FIGURE 1

FIGURE 1. From: Role of the β-Subunit Arginine/Lysine Finger in Integrin Heterodimer Formation and Function.

Structure and conservation of the Arg/Lys finger in integrin β-subunits. A, Three-dimensional crystal structure of unliganded integrin αVβ3 head segment (as a ribbon diagram with the αV propeller domain in blue and the βA domain in red) showing the position of the arginine finger (Arg261, carbon atoms in green, amides in blue) projecting from the 310 helix. Loop 3 (long arrow) and the ADMIDAS cation (magenta sphere, short arrow) are indicated. The four metal ions at the base of the propeller are indicated as orange spheres. B, Higher magnification of the Arg/Lys coordination pocket, with a portion of the aromatic side chains forming the upper ring of the cup-like “cage” structure of αV propeller (adapted from Refs. 7 and 33). Orientation is the same as in A. C, Structure alignment of all eight mammalian β-subunits around the Arg/Lys finger (boxed). The amino acid sequence of strands βD and βD′, loop 3 and the 310 helix are indicated in single letter code. The β4-subunit structure model was generated using Modeler (34) with the αVβ3 structure (PDB code: 1jv2) as template.

Vineet Gupta, et al. J Immunol. ;180(3):1713-1718.

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