Binding of ISRIB reveals a regulatory site in the nucleotide exchange factor eIF2B | Zendy

Alisa Zyryanova | Zendy; Félix Weis | Zendy; Alexandre Faille | Zendy; Akeel Abo Alard | Zendy; Ana Crespillo-Casado | Zendy; Yusuke Sekine | Zendy; Heather P. Harding | Zendy; Felicity Allen | Zendy; Leopold Parts | Zendy; Christophe Fromont | Zendy; Peter M. Fischer | Zendy; Alan J. Warren | Zendy; David Ron | Zendy

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Binding of ISRIB reveals a regulatory site in the nucleotide exchange factor eIF2B

Author(s) -

Alisa Zyryanova,

Félix Weis,

Alexandre Faille,

Akeel Abo Alard,

Ana Crespillo-Casado,

Yusuke Sekine,

Heather P. Harding,

Felicity Allen,

Leopold Parts,

Christophe Fromont,

Peter M. Fischer,

Alan J. Warren,

David Ron

Publication year - 2018

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aar5129

Subject(s) - a site , translation (biology) , binding site , biology , biophysics , microbiology and biotechnology , chemistry , computational biology , biochemistry , gene , messenger rna

ISRIB mechanism of action In rodents, a druglike small molecule named ISRIB enhances cognition and reverses cognitive deficits after traumatic brain injury. ISRIB activates a protein complex called eIF2B that is required for the synthesis of new proteins. Tsaiet al. report the visualization of eIF2B bound to ISRIB at near-atomic resolution by cryo–electron microscopy. Biochemical studies revealed that ISRIB is a “molecular staple” that promotes assembly of the fully active form of eIF2B. Zyryanovaet al. report similar structures together with information on the binding of ISRIB analogs and their effects on protein translation.Science , this issue p.eaaq0939 , p.1533

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