23nx: Difference between revisions

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'''Unreleased structure'''


The entry 23nx is ON HOLD  until Paper Publication
==Structure of mouse DNMT3A-TCL1A complex==
<StructureSection load='23nx' size='340' side='right'caption='[[23nx]], [[Resolution|resolution]] 3.32&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[23nx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=23NX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=23NX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.32&#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=23nx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=23nx OCA], [https://pdbe.org/23nx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=23nx RCSB], [https://www.ebi.ac.uk/pdbsum/23nx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=23nx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TCL1A_MOUSE TCL1A_MOUSE] Enhances the phosphorylation and activation of AKT1 and AKT2. Enhances cell proliferation, stabilizes mitochondrial membrane potential and promotes cell survival (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DNA methyltransferase DNMT3A is a key enzyme responsible for establishing DNA methylation patterns during mammalian development. T-cell leukemia/lymphoma 1 A (TCL1A) is a proto-oncogene expressed mainly in embryonic and fetal tissues, as well as in specific lymphocyte populations. In this study, we determined the structure of the murine DNMT3A-TCL1A complex using single-particle cryo-electron microscopy. The complex adopts a linear conformation, with two TCL1A dimers bound to the catalytic domain of DNMT3A to form a heterohexamer. TCL1A competitively binds to the same structural interface on DNMT3A as DNMT3L, but produces an inhibitory-rather than an activating-effect on the catalytic activity of DNMT3A. Furthermore, comparative analysis with previously reported assembly modes of murine TCL1A revealed that the TCL1A dimer complex we resolved adopts distinct molecular conformations and interaction mechanisms. Our findings elucidate the allosteric mechanism by which murine TCL1A inhibits DNMT3A activity, providing a structural basis for understanding mammalian epigenetic reprogramming.


Authors:  
Cryo-EM structure of the murine DNMT3A-TCL1A complex.,Li W, Liu Q, Li J, Wang X, He G, Guo L J Struct Biol. 2026 Aug 3;218(3):108352. doi: 10.1016/j.jsb.2026.108352. PMID:42546996<ref>PMID:42546996</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 23nx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Guo L]]
[[Category: He G]]
[[Category: Li J]]
[[Category: Li W]]
[[Category: Liu Q]]
[[Category: Wang X]]
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