Display Settings:

Items per page

Results: 8

1.
Figure 3

Figure 3. From: An Initial Event in Insect Innate Immune Response: Structural and Biological Studies of Interactions between ?-1,3-glucan and the N-terminal Domain of ?-1,3-glucan Recognition Protein.

1H-15N HSQC spectra of N-βGRP (0.5 mM) in the absence (left) or presence (right) of laminarin (1 mM) at 25°C, pH 6.5.

Huaien Dai, et al. Biochemistry. ;52(1):161-170.
2.
Figure 7

Figure 7. From: An Initial Event in Insect Innate Immune Response: Structural and Biological Studies of Interactions between ?-1,3-glucan and the N-terminal Domain of ?-1,3-glucan Recognition Protein.

A schematic representation of formation of N-βGRP: β-1,3-glucan macro complex: (A) Laminarin binding to N-βGRP and self-association of N-βGRP:laminarin complex; (B) & (C) N-βGRP packing and concomitant electrostatic interactions as can be observed in the crystal structure of N-βGRP:laminarihexaose (12). Negative and positive potential surfaces are shown in red and blue, respectively.

Huaien Dai, et al. Biochemistry. ;52(1):161-170.
3.
Figure 4

Figure 4. From: An Initial Event in Insect Innate Immune Response: Structural and Biological Studies of Interactions between ?-1,3-glucan and the N-terminal Domain of ?-1,3-glucan Recognition Protein.

Effect of addition of varying concentrations of laminarin on N-βGRP, as monitored by sedimentation velocity experiments: Sedimentation profiles of N-βGRP (26.2 μM) in the absence (A) or presence of different levels of laminarin (B–H). Sedimentation at 49,000 rpm and 20 °C was monitored by measuring absorbance at 280 nm.

Huaien Dai, et al. Biochemistry. ;52(1):161-170.
4.
Figure 5

Figure 5. From: An Initial Event in Insect Innate Immune Response: Structural and Biological Studies of Interactions between ?-1,3-glucan and the N-terminal Domain of ?-1,3-glucan Recognition Protein.

Effect of dilution on N-βGRP:laminarin complex as monitored by sedimentation velocity profiles: (A) 34 μM N-βGRP and 780 μM laminarin at 280 nm; (B) 3.4 μM N-βGRP and 78 μM laminarin at 220 nm; (C) 0.68 μM N-βGRP and 15.6 μM laminarin at 205 nm. The concentration ratio of N-βGRP:laminarin was maintained at 1:22.9. Sedimentation was carried out at 49,000 rpm and 20°C.

Huaien Dai, et al. Biochemistry. ;52(1):161-170.
5.
Figure 6

Figure 6. From: An Initial Event in Insect Innate Immune Response: Structural and Biological Studies of Interactions between ?-1,3-glucan and the N-terminal Domain of ?-1,3-glucan Recognition Protein.

Sedimentation velocity profiles for N-βGRP, laminarin and their mixtures, as monitored at 49,000 rpm and 20°C by absorbance at 280 nm (A–C) and interference optics (D–F) at 5 min. intervals: 75 μM N-βGRP (A & D) and 125 μM laminarin (B & E) were sedimented separately or together (C & F). Fringe displacements in D–F are given in arbitrary units.

Huaien Dai, et al. Biochemistry. ;52(1):161-170.
6.
Figure 2

Figure 2. From: An Initial Event in Insect Innate Immune Response: Structural and Biological Studies of Interactions between ?-1,3-glucan and the N-terminal Domain of ?-1,3-glucan Recognition Protein.

Mapping of ligand-binding site on P. interpunctella N-βGRP by NMR titration of 1H-15 laminarihexaose at 25°C, pH 6.5: (A) N HSQC spectra of N-βGRP (0.5 mM) in the absence (black) or presence (red) of laminarihexaose (3 mM); (B) Chemical shift changes undergone by the backbone 15N-1H groups; the weighted average of chemical shift changes of an 15N-1H group was calculated by using the formula, [(ΔH2+(ΔN/5)2)/2]1/2, where ΔH and ΔN represent 1H and 15N chemical shift change, respectively; (C) Residues undergoing a chemical shift perturbation of > 0.02 ppm upon laminarihexaose titration are shown in red.

Huaien Dai, et al. Biochemistry. ;52(1):161-170.
7.
Figure 1

Figure 1. From: An Initial Event in Insect Innate Immune Response: Structural and Biological Studies of Interactions between ?-1,3-glucan and the N-terminal Domain of ?-1,3-glucan Recognition Protein.

(A) Superimposition of ribbon structures of N-βGRP from several insects: P. interpunctella - purple, 2KHA (NMR, current work); B. mori - gray, 2RQE [NMR; (11)]; D. melanogaster - green, 3IE4 [X-ray; (13)]; B. mori (laminarihexaose-bound) – orange, 3AQX [X-ray; (12)]; P. interpunctella - blue, 3AQY [X-ray; (12)]; P. interpunctella (laminarihexaose-bound) - red, 3AQZ [X-ray; (12)]; The NMR structure of P. interpunctella N-βGRP reported here differs from that of the B. mori protein (11) in the configuration of a Pro, as indicated. (B) Ensemble of twenty lowest-energy structures of P. interpunctella N-βGRP (2KHA). (C) A plot of backbone heteronuclear {15N}-1H NOE values vs. residue number for P. interpunctella N-βGRP. Pro residues do not give rise to {15N}-1H NOEs. A couple of C-terminal residues had hetero NOE peak intensities barely above the noise level. Each β-strand is represented by an arrow.

Huaien Dai, et al. Biochemistry. ;52(1):161-170.
8.
Figure 8

Figure 8. From: An Initial Event in Insect Innate Immune Response: Structural and Biological Studies of Interactions between ?-1,3-glucan and the N-terminal Domain of ?-1,3-glucan Recognition Protein.

Electrostatic interactions play a role in the formation of N-βGRP: β-1,3-glucan macro complex: (A) Sedimentation velocity profiles for N-βGRP (wide type, black; D45A, blue; and D45K, red) in the presence of laminarin; Activation of the prophenoloxidase pathway by N- βGRP and mutants without (B) or with laminarin (C). Samples of plasma (5 μl) were mixed with protein alone or with protein and laminarin. After incubation at room temperature for 15 min, phenoloxidase activity was measured using dopamine hydrochloride as a substrate, as described under “Experimental Procedures”. The bars represent the means ± S.E. of data from three sets of measurements on a pooled plasma sample. Bars labeled with different letters (a, b, and c) are significantly different [analysis of variance (ANOVA), p < 0.05].

Huaien Dai, et al. Biochemistry. ;52(1):161-170.

Display Settings:

Items per page

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk