Table 3 Project hope mutation (1|P01130|LDLR_HUMAN) to predict the effect of the LDLR mutations on the structure and function of the LDLR protein (Venselaar et al., 2010)
Variant | Amino acid charge | Size of the mutant amino acid | Hydrophobicity of mutant residue | Effect on the protein structure and prediction of the expected effect on function | |
|---|---|---|---|---|---|
Wild type residue | Mutant type residue | ||||
c.514G > A (p.D172N) | Negative | Neutral | The same | No change | - The mutation of aspartic Acid into asparagine at position 172 - Probably not damaging to the protein (Based on conservation information) - The mutated residue is located very close to a residue that makes a cysteine bond. This cysteine bond itself is not mutated but could be affected by the mutation located in its vicinity - Because the negative charge is lost the interaction with the metal will be less stable, this can disturb the domain |
c.532G > A (p.D178N) | Negative | Neutral | The same | No change | - The mutation of aspartic Acid into asparagine at position 178 - Probably damaging to the protein (Based on conservation information) - Because the negative charge is lost the interaction with the metal will be less stable, this can disturb the domain |
c.418G > T (p.E140*) | Expresses a premature stop codon at position 140 and consequently a truncated LDLR protein is produced, which is a defective LDL receptor | ||||
C404 T > A (p.L135*) | Expresses a premature stop codon at position 135 and consequently, a truncated LDLR protein is produced which is a defective LDL receptor | ||||