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4CRW

Complex of human DDX6 (RECA-C) and CNOT1 (MIF4G)

Summary for 4CRW
Entry DOI10.2210/pdb4crw/pdb
Related2WAX 2WAY 4GMJ 4GML
DescriptorCCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT 1, PROBABLE ATP-DEPENDENT RNA HELICASE DDX6, GLYCEROL, ... (4 entities in total)
Functional Keywordsgene regulation, ccr4-not, translational repression, mrna decapping, dead-box protein, p54, rck, helicase, mrna silencing, mrna deadenylation, eif4a, translation, mirna, p-bodies
Biological sourceHOMO SAPIENS (HUMAN)
More
Cellular locationCytoplasm, P-body: A5YKK6 P26196
Total number of polymer chains2
Total formula weight48553.90
Authors
Chen, Y.,Boland, A.,Izaurralde, E.,Weichenrieder, O. (deposition date: 2014-03-01, release date: 2014-05-07, Last modification date: 2023-12-20)
Primary citationChen, Y.,Boland, A.,Kuzuoglu-Ozturk, D.,Bawankar, P.,Loh, B.,Chang, C.T.,Weichenrieder, O.,Izaurralde, E.
A Ddx6-Cnot1 Complex and W-Binding Pockets in Cnot9 Reveal Direct Links between Mirna Target Recognition and Silencing
Mol.Cell, 54:737-, 2014
Cited by
PubMed Abstract: CCR4-NOT is a major effector complex in miRNA-mediated gene silencing. It is recruited to miRNA targets through interactions with tryptophan (W)-containing motifs in TNRC6/GW182 proteins and is required for both translational repression and degradation of miRNA targets. Here, we elucidate the structural basis for the repressive activity of CCR4-NOT and its interaction with TNRC6/GW182s. We show that the conserved CNOT9 subunit attaches to a domain of unknown function (DUF3819) in the CNOT1 scaffold. The resulting complex provides binding sites for TNRC6/GW182, and its crystal structure reveals tandem W-binding pockets located in CNOT9. We further show that the CNOT1 MIF4G domain interacts with the C-terminal RecA domain of DDX6, a translational repressor and decapping activator. The crystal structure of this complex demonstrates striking similarity to the eIF4G-eIF4A complex. Together, our data provide the missing physical links in a molecular pathway that connects miRNA target recognition with translational repression, deadenylation, and decapping.
PubMed: 24768540
DOI: 10.1016/J.MOLCEL.2014.03.034
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

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数据于2024-11-06公开中

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