Table 1 Mutational analysis of the C-terminal hydrophobic region (Val245 to Val256) of ricin A-chain
RTA decreased hydrophobicity | ||||
|---|---|---|---|---|
Position in RTA, C-terminal region | Primary residue | Altered residue | Comments | |
Uncharged | Charged | |||
245 | Val (V) | Ser (S) | - | Suggested |
247 | Ile (I) | Asn (N) | Asp (D) | Not recommended, might disrupt RTA fold |
248 | Leu (L) | Asn (N) | Asp (D) | Asp may change RTA interactions, Asn suggested |
249 | Ile (I) | Asn (N) | Asp (D) | Not recommended, might disrupt fold and affect interaction with B-chain |
250 | Pro (P) | Ala (A) | - | Not recommended, Ala changes the structure of RTA [23] |
251 | Ile (I) | Asn (N) | Asp (D) | Not recommended, affects interaction with B-chain |
252 | Ile (I) | Asn (N) | Asp (D) | Asp may change RTA interactions, Asn suggested |
253 | Ala (A) | Ser (S) | - | Suggested |
254 | Leu (L) | Asn (N) | Asp (D) | Not recommended, might disrupt RTA fold |
255 | Met (M) | Gln (Q) | Lys (L) | Not recommended, might disrupt RTA fold |
256 | Val (V) | Ser (S) | - | Not recommended, might disrupt RTA fold |
RTA increased hydrophobicity | ||||
Position in RTA, C-terminal region | Primary residue | Altered residue | Comments | |
Uncharged | Charged | |||
246 | Ser (S) | Val (V) | - | Suggested |
253 | Ala (A) | Val (V) | - | Suggested |