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Table 1.

Summary of all software used to find out harmful missense SNPs and their impact on CD-209 model.

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Table 1 Expand

Table 2.

List of 27 most deleterious missense SNPs along with their software scores.

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Table 2 Expand

Table 3.

Results for PCFA1, PCFA2, and ZCA-cor composite scores.

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Table 3 Expand

Fig 1.

Receiver Operator Characteristic (ROC) curves for 3 logistical regression models.

Full model (blue curve): PCFA2 and ZCA-cor composite scores are predictors. PCFA2 Model (red curve). ZCA-cor Model (green curve).

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Fig 1 Expand

Table 4.

Area under the curve per model with their 95% confidence intervals.

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Table 4 Expand

Fig 2.

Complete 3D structure simulated by I-TASSER.

Complete CD209 structure is colored according to secondary protein structures. In this structure, red color shows the location of alpha-helixes and turquoise of beta-sheets. The one part with yellows color represents the C-Lectin domain involved in ligand binding.

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Fig 2 Expand

Fig 3.

Ramachandran plot of complete model.

This model shows the number of residues in the favored, allowed and outlier region. As mostly glycine has two hydrogen atoms attached to its side chain so if it lies in outlier region, it does not affect the overall 3D structure.

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Fig 3 Expand

Table 5.

Effect of deleterious SNPs on protein stability along with their solubility, charge and polarity properties.

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Table 5 Expand

Table 6.

Ramachandran analysis of all the mutated models in addition to evolutionary conservation score predicted by ConSurf.

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Table 6 Expand

Fig 4.

Hydrogen bonds and other interaction created by substituted amino acid at 320 and 366 positions in CD-209.

The substituted amino acids are represented in green color, which form interaction with other surrounding residues colored differently. Moreover, green color is also selected to indicate hydrogen bond, whereas other bond colors represents other hydrophobic or electrostatic interactions.

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Fig 4 Expand

Fig 5.

Replacement of Glycine at 265, 317 and 346 positions with respective residues and their hydrophobic and hydrogen bonds interactions.

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Fig 5 Expand

Fig 6.

Hydrogen bonds, hydrophobic and electrostatic interaction of substituted amino acids at 318 and 348 positions.

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Fig 6 Expand

Fig 7.

Hydrogen bond and other hydrophobic and electrostatic interactions created by substituted residues at 260, 315 and 343 positions in CD-209 model.

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Fig 7 Expand