View source for 7obp


==Crystal structure of the human NCOA7-AS TLDc domain==
<StructureSection load='7obp' size='340' side='right'caption='[[7obp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7obp]] is a 6 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=7OBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OBP 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]] 1.8&#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=7obp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7obp OCA], [https://pdbe.org/7obp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7obp RCSB], [https://www.ebi.ac.uk/pdbsum/7obp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7obp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NCOA7_HUMAN NCOA7_HUMAN] Enhances the transcriptional activities of several nuclear receptors. Involved in the coactivation of different nuclear receptors, such as ESR1, THRB, PPARG and RARA.<ref>PMID:11971969</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The TLDc [Tre2/Bub2/Cdc16 (TBC), lysin motif (LysM), domain catalytic] domain is associated with oxidation-resistance related functions and is well conserved among eukaryotes. Seven proteins possess a TLDc domain in humans, notably proteins belonging to the oxidation resistance protein (OXR), nuclear receptor coactivator 7 (NCOA7) and TBC1 domain family member 24 (TBC1D24) families. Although the mechanism is unknown, a protective role of TLDc proteins against oxidative stress, notably in the brain, has been demonstrated. Neurobiological disorders caused by mutations in the TLDc domain have also been reported. The human NCOA7 gene encodes several mRNA isoforms; among these, isoform 4, named NCOA7-AS, is up-regulated by type 1 interferon in response to viral infection. NCOA7 and NCOA7-AS both interact with several subunits of the vacuolar proton pump V-ATPase, which leads to increased acidification of the endolysosomal system and consequently impairs infection by viruses that enter their host cells through the endosomal pathway, such as influenza A virus and hepatitis C virus. Similarly to full-length NCOA7, NCOA7-AS possesses a TLDc domain in its C-terminus. Structures of TLDc domains have been reported from zebrafish and fly but not from humans. Here, the expression, purification and crystallization of the TLDc domain from NCOA7 and NCOA7-AS is reported. The crystal structure solved at 1.8 A resolution is compared with previously solved three-dimensional structures of TLDc domains.

Crystal structure of the TLDc domain of human NCOA7-AS.,Arnaud-Arnould M, Tauziet M, Moncorge O, Goujon C, Blaise M Acta Crystallogr F Struct Biol Commun. 2021 Aug 1;77(Pt 8):230-237. doi:, 10.1107/S2053230X21006853. Epub 2021 Jul 28. PMID:34341188<ref>PMID:34341188</ref>

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