2014Unpublished venueRequires access

The Structure and Action of Ribosome‐inactivating Proteins

Jon D. Robertus, A.F. Monzingo

Open publisher page 8 citations

Abstract

Ribosome-inhibiting proteins, RIPs, are widespread in nature and include plant cytotoxins like ricin as well as bacterial toxins, like those from Shigella. RIPs act by depurinating an invariant adenine from rRNA and thereby inhibiting protein synthesis; they have evolved to near enzymatic perfection. The X-ray structures of RIPs have allowed this exquisite mechanism to be understood. Furthermore, knowledge of the structure has facilitated the design of specific inhibitors that may be useful as drugs in the future.

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What this paper is about

Ribosome-inhibiting proteins, RIPs, are widespread in nature and include plant cytotoxins like ricin as well as bacterial toxins, like those from Shigella. RIPs act by depurinating an invariant adenine from rRNA and thereby inhibiting protein synthesis; they have evolved to near enzymatic perfection. The X-ray structures of RIPs have allowed this exquisite mechanism to be understood. Furthermore, knowledge of the structure has facilitated the design of specific inhibitors that may be useful as drugs in the future.

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Available abstract

Ribosome-inhibiting proteins, RIPs, are widespread in nature and include plant cytotoxins like ricin as well as bacterial toxins, like those from Shigella. RIPs act by depurinating an invariant adenine from rRNA and thereby inhibiting protein synthesis; they have evolved to near enzymatic perfection. The X-ray structures of RIPs have allowed this exquisite mechanism to be understood. Furthermore, knowledge of the structure has facilitated the design of specific inhibitors that may be useful as drugs in the future.

Key concepts: Ribosome-inactivating protein, Ricin, Ribosome, Protein biosynthesis, Chemistry, Computational biology, Mechanism of action, Biochemistry

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