1q1v

<StructureSection load='1q1v' size='340' side='right'caption='[[1q1v]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1q1v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q1V FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dek ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

[[https://www.uniprot.org/uniprot/DEK_HUMAN DEK_HUMAN]] Note=A chromosomal aberration involving DEK is found in a subset of acute myeloid leukemia (AML); also known as acute non-lymphocytic leukemia. Translocation t(6;9)(p23;q34) with NUP214/CAN. It results in the formation of a DEK-CAN fusion gene.

[[https://www.uniprot.org/uniprot/DEK_HUMAN DEK_HUMAN]] Involved in chromatin organization.<ref>PMID:17524367</ref>

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== Publication Abstract from PubMed ==

The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these clinical connections has yet to be explained. We have identified a structural domain in the C-terminal region of DEK [DEK(309-375)]. DEK(309-375) implies clinical importance because it can reverse the characteristic abnormal DNA-mutagen sensitivity in fibroblasts from ataxia-telangiectasia (A-T) patients. We determined the solution structure of DEK(309-375) by nuclear magnetic resonance spectroscopy, and found it to be structurally homologous to the E2F/DP transcription factor family. On the basis of this homology, we tested whether DEK(309-375) could bind DNA and identified the DNA-interacting surface. DEK presents a hydrophobic surface on the side opposite the DNA-interacting surface. The structure of the C-terminal region of DEK provides insights into the protein function of DEK.

Solution NMR structure of the C-terminal domain of the human protein DEK.,Devany M, Kotharu NP, Matsuo H Protein Sci. 2004 Aug;13(8):2252-9. Epub 2004 Jul 6. PMID:15238633<ref>PMID:15238633</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1q1v" style="background-color:#fffaf0;"></div>

[[Category: Human]]

[[Category: Devany, M]]

[[Category: Kotharu, N P]]

[[Category: Matsuo, H]]

[[Category: Winged-helix motif]]