Table 6.

Depicts the structural impact of TLR3 mutations retrieved from the HOPE server.

N284I	C37R	L360P
Mutant and wild-type amino acids differ in size.	Mutants have differing charges than wild-type amino acids.	The mutant and wild-type amino acids differ in size.
Wild-type residue is less compact than mutant.	The mutant residue charges a buried residue, which may disrupt protein folding.	Compared to wild-type, mutant residues are compact.
Mutations empty the protein’s core.
Mutant and wild-type residues differ hydrophobically.	Mutant and wild-type amino acids differ in size.	The mutation will empty the protein’s core.
Mutations weaken core hydrogen bonding, preventing folding.	Wild-type residue is smaller than mutant residue.	The altered residue is near another binding site and in a protein-critical domain.
The altered residue is near a binding site and protein-critical domain.	The protein’s core hid the wild-type residue. Due to its size, the mutant residue may not fit.	The mutation may prevent signal transmission between these sites.
These domains may interact differently due to the mutation, altering signal transmission.	Mutant and wild-type residues differ hydrophobically.	The altered residue is near other domain residues and in a protein-critical area, and this interaction may be essential for protein function.
The changed residue is near domain residues and protein-critical.	The mutation removes hydrophobic contacts from the protein’s core.
Common Interferences:
The mutation may impact this protein interaction, preventing protein function.
The mutant residue is near a protein domain which is essential to its activity.
The mutation may affect how these domains interact, affecting protein function.