5anr

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==4E-T - DDX6 - CNOT1 complex==
==4E-T - DDX6 - CNOT1 complex==
<StructureSection load='5anr' size='340' side='right' caption='[[5anr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5anr' size='340' side='right' caption='[[5anr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CNOT1_HUMAN CNOT1_HUMAN]] Belongs to the CCR4-NOT complex that functions as general transcription regulation complex. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors.<ref>PMID:10637334</ref> <ref>PMID:16778766</ref> [[http://www.uniprot.org/uniprot/4ET_HUMAN 4ET_HUMAN]] Nucleoplasmic shuttling protein. Mediates the nuclear import of EIF4E by a piggy-back mechanism. [[http://www.uniprot.org/uniprot/DDX6_HUMAN DDX6_HUMAN]] In the process of mRNA degradation, may play a role in mRNA decapping.
[[http://www.uniprot.org/uniprot/CNOT1_HUMAN CNOT1_HUMAN]] Belongs to the CCR4-NOT complex that functions as general transcription regulation complex. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors.<ref>PMID:10637334</ref> <ref>PMID:16778766</ref> [[http://www.uniprot.org/uniprot/4ET_HUMAN 4ET_HUMAN]] Nucleoplasmic shuttling protein. Mediates the nuclear import of EIF4E by a piggy-back mechanism. [[http://www.uniprot.org/uniprot/DDX6_HUMAN DDX6_HUMAN]] In the process of mRNA degradation, may play a role in mRNA decapping.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The DEAD-box protein DDX6 is a central component of translational repression mechanisms in maternal mRNA storage in oocytes and microRNA-mediated silencing in somatic cells. DDX6 interacts with the CCR4-NOT complex and functions in concert with several post-transcriptional regulators, including Edc3, Pat1, and 4E-T. We show that the conserved CUP-homology domain (CHD) of human 4E-T interacts directly with DDX6 in both the presence and absence of the central MIF4G domain of CNOT1. The 2.1-A resolution structure of the corresponding ternary complex reveals how 4E-T CHD wraps around the RecA2 domain of DDX6 and contacts CNOT1. Although 4E-T CHD lacks recognizable sequence similarity with Edc3 or Pat1, it shares the same DDX6-binding surface. In contrast to 4E-T, however, the Edc3 and Pat1 FDF motifs dissociate from DDX6 upon CNOT1 MIF4G binding in vitro. The results underscore the presence of a complex network of simultaneous and/or mutually exclusive interactions in DDX6-mediated repression.
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Structure of a Human 4E-T/DDX6/CNOT1 Complex Reveals the Different Interplay of DDX6-Binding Proteins with the CCR4-NOT Complex.,Ozgur S, Basquin J, Kamenska A, Filipowicz W, Standart N, Conti E Cell Rep. 2015 Oct 27;13(4):703-11. doi: 10.1016/j.celrep.2015.09.033. Epub 2015 , Oct 17. PMID:26489469<ref>PMID:26489469</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5anr" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 16:23, 10 May 2016

4E-T - DDX6 - CNOT1 complex

5anr, resolution 2.10Å

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