Work

Author response: Didemnin B and ternatin-4 differentially inhibit conformational changes in eEF1A required for aminoacyl-tRNA accommodation into mammalian ribosomes

Year: 2022

Type: peer-review

Abstract: Cyclic peptide natural products didemnin B and ternatin-4 bind the same hydrophobic pocket of eEF1A to inhibit mRNA translation but exhibit kinetic differences that influence rate-limiting conformational changes underpinning aminoacyl-tRNA selection.

DOI: 10.7554/elife.81608.sa2

Authors: Manuel F Juette, Jordan D Carelli, Emily J Rundlet, Alan Brown, Sichen Shao, Angelica Ferguson, Michael R Wasserman, Mikael Holm, Jack Taunton, Scott C Blanchard

Institutions: Weill Cornell Medicine, University of California, San Francisco, St. Jude Children's Research Hospital, Tri-Institutional PhD Program in Chemical Biology

Language: English

Topic: RNA and protein synthesis mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

OpenAlex ID: W4306952685

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