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. 2019 Jun 18;11(6):350. doi: 10.3390/toxins11060350

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Crystal structures of ricin A-chain. PDB protein data bank (code 2AA1). Whole ricin A-chain (RTA) structures are marked in red. The hydrophobic region (Val245 to Val256) is indicated in purple. Several residues have been selected within the hydrophobic region and modified to obtain RTA with changed secondary structure or changed hydrophobicity. These residues are: (A) P250 (marked in yellow) has been modified (P250A) to produce RTA with a changed secondary structure; (B) V245, L248, I252, and A253 (marked in orange) have been modified (V245S, L248N, I252N, A253S) to obtain RTA with decreased hydrophobicity (RTA DHF); (C) S246 and A253 (marked in green) have been changed (S246V, A253V) to obtain RTA with increased hydrophobicity (RTA IHF).