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Table 1 Mutational analysis of the C-terminal hydrophobic region (Val245 to Val256) of ricin A-chain

From: Hydrophobicity of protein determinants influences the recognition of substrates by EDEM1 and EDEM2 in human cells

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
  1. Mutations that were chosen to be introduced into this region are marked in bold.