View source for 7voi


==Structure of the human CNOT1(MIF4G)-CNOT6L-CNOT7 complex==
<StructureSection load='7voi' size='340' side='right'caption='[[7voi]], [[Resolution|resolution]] 4.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7voi]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VOI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.38&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7voi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7voi OCA], [https://pdbe.org/7voi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7voi RCSB], [https://www.ebi.ac.uk/pdbsum/7voi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7voi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CNOT7_HUMAN CNOT7_HUMAN] Ubiquitous transcription factor required for a diverse set of processes. It is a component of the CCR4 complex involved in the control of gene expression (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Regulated degradation of mature, cytoplasmic mRNA is a key step in eukaryotic gene regulation. This process is typically initiated by the recruitment of deadenylase enzymes by cis-acting elements in the 3' untranslated region resulting in the shortening and removal of the 3' poly(A) tail of the target mRNA. The Ccr4-Not complex, a major eukaryotic deadenylase, contains two exoribonuclease subunits with selectivity toward poly(A): Caf1 and Ccr4. The Caf1 deadenylase subunit binds the MIF4G domain of the large subunit CNOT1 (Not1) that is the scaffold of the complex. The Ccr4 nuclease is connected to the complex via its leucine-rich repeat (LRR) domain, which binds Caf1, whereas the catalytic activity of Ccr4 is provided by its EEP domain. While the relative positions of the MIF4G domain of CNOT1, the Caf1 subunit, and the LRR domain of Ccr4 are clearly defined in current models, the position of the EEP nuclease domain of Ccr4 is ambiguous. Here, we use X-ray crystallography, the AlphaFold resource of predicted protein structures, and pulse electron paramagnetic resonance spectroscopy to determine and validate the position of the EEP nuclease domain of Ccr4 resulting in an improved model of the human Ccr4-Not nuclease module.

Structure of the human Ccr4-Not nuclease module using X-ray crystallography and electron paramagnetic resonance spectroscopy distance measurements.,Zhang Q, Pavanello L, Potapov A, Bartlam M, Winkler GS Protein Sci. 2022 Mar;31(3):758-764. doi: 10.1002/pro.4262. Epub 2022 Jan 7. PMID:34923703<ref>PMID:34923703</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7voi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bartlam M]]
[[Category: Zhang Q]]