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Structural basis for chaperone-guided assembly of RNA-induced silencing complex

This article presents a scientific study detailing the structural basis for the chaperone-guided assembly of the RNA-induced silencing complex (RISC). It describes the deposition of cryo-electron microscopy (cryo-EM) structures and maps into public databases such as the Protein Data Bank (PDB) and Electron Microscopy Data Bank (EMDB). The research focuses on the interaction between molecular chaperones like HSP90 and components of the RISC complex, including Ago2 and let-7a-1. The study builds upon previous work published in journals such as Molecular Cell and Nature Structural & Molecular生物学.

Data availability

The cryo-EM structure of AMC–let-7a-1 has been deposited in the PDB under accession code 9W5I . The composite map and consensus map of AMC–let-7a-1 have been deposited in the EMDB under accession codes EMD-65663 and EMD-65662 , respectively. The partial maps of local refinement focused on MID/PIWI, N-domain and HSP90–p23 have been deposited in the EMDB under accession codes EMD-65661 , EMD-65660 and EMD-65659 , respectively. The consensus map and AGO2-focused map of AMC have been deposited in the EMDB under accession codes EMD-69544 and EMD-65658 , respectively. There are no restrictions on data availability. For material requests, please contact the corresponding authors. Other structural models cited in this study for analysis ( 4W5N , 4W5O , 7KRJ , 7XW2 , 8EOB , 9CMP , 7V6C , 7ZUB , 8FFW , 5FWK , 5FWL , 7Z37 and 8GFT ) are also available at the PDB.

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Source document: Hsc70/Hsp90 chaperone machinery mediates ATP-dependent RISC loading of small RNA duplexes

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Nature NewsParty-alignedCenter11 days ago
Structural basis for chaperone-guided assembly of RNA-induced silencing complex

This article presents a scientific study detailing the structural basis for the chaperone-guided assembly of the RNA-induced silencing complex (RISC). It describes the deposition of cryo-electron microscopy (cryo-EM) structures and maps into public databases such as the Protein Data Bank (PDB) and Electron Microscopy Data Bank (EMDB). The research focuses on the interaction between molecular chaperones like HSP90 and components of the RISC complex, including Ago2 and let-7a-1. The study builds upon previous work published in journals such as Molecular Cell and Nature Structural & Molecular生物学.

Bias read (Center): The article is purely scientific and does not present any political, social, or ideological content. It focuses on biological mechanisms and provides technical details about data availability and prior research without taking a stance or showing bias.

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