View source for 2mbh


==NMR structure of EKLF(22-40)/Ubiquitin Complex==
<StructureSection load='2mbh' size='340' side='right'caption='[[2mbh]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mbh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MBH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbh OCA], [https://pdbe.org/2mbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mbh RCSB], [https://www.ebi.ac.uk/pdbsum/2mbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mbh ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/KLF1_HUMAN KLF1_HUMAN] Hereditary persistence of fetal hemoglobin - beta-thalassemia;Hereditary persistence of fetal hemoglobin - sickle cell disease;Congenital dyserythropoietic anemia due to KLF1 mutation. Congenital dyserythropoietic anemia 4 (CDA4) [MIM:[https://omim.org/entry/613673 613673]: A blood disorder characterized by ineffective erythropoiesis and hemolysis resulting in anemia. Circulating erythroblasts and erythroblasts in the bone marrow show various morphologic abnormalities. Affected individuals with CDA4 also have increased levels of fetal hemoglobin. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:21055716</ref> 
== Function ==
[https://www.uniprot.org/uniprot/KLF1_HUMAN KLF1_HUMAN] Transcription regulator of erythrocyte development that probably serves as a general switch factor during erythropoiesis. Is a dual regulator of fetal-to-adult globin switching. Binds to the CACCC box in the beta-globin gene promoter and acts as a preferential activator of this gene. Furthermore, it binds to the BCL11A promoter and activates expression of BCL11A, which in turn represses the HBG1 and HBG2 genes. This dual activity ensures that, in most adults, fetal hemoglobin levels are low. Able to activate CD44 and AQP1 promoters. When sumoylated, acts as a transcriptional repressor by promoting interaction with CDH2/MI2beta and also represses megakaryocytic differentiation (By similarity).<ref>PMID:21055716</ref> <ref>PMID:20676099</ref> 
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== Publication Abstract from PubMed ==
Like other acidic transactivation domains (TAD), the minimal TAD from the erythroid-specific transcription factor EKLF (EKLFTAD) has been shown to contribute both to its transcriptional activity as well as to its ubiquitin(UBI)-mediated degradation. In this article, we examine the activation-degradation role of the acidic TAD of EKLF and demonstrate that the first 40 residues (EKLFTAD1) within this region form a noncovalent interaction with UBI. Nuclear magnetic resonance (NMR) structural studies of an EKLFTAD1-UBI complex show that EKLFTAD1 adopts a 14-residue alpha helix that forms the recognition interface with UBI in a similar manner as the UBI-interacting helix of Rabex5. We also identify a similar interaction between UBI and the activation-degradation region of SREBP1a, but not with the activation-degradation regions of p53, GAL4, and VP16. These results suggest that select activation-degradation regions like the ones found in EKLF and SREBP1a function in part through their ability to form noncovalent interactions with UBI.

Structural Characterization of a Noncovalent Complex between Ubiquitin and the Transactivation Domain of the Erythroid-Specific Factor EKLF.,Raiola L, Lussier-Price M, Gagnon D, Lafrance-Vanasse J, Mascle X, Arseneault G, Legault P, Archambault J, Omichinski JG Structure. 2013 Nov 5;21(11):2014-24. doi: 10.1016/j.str.2013.08.027. Epub 2013, Oct 17. PMID:24139988<ref>PMID:24139988</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mbh" style="background-color:#fffaf0;"></div>

==See Also==
*[[3D structures of ubiquitin|3D structures of ubiquitin]]
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Omichinski JG]]
[[Category: Raiola L]]