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10.1038/leu.2014.111 http://scihub22266oqcxt.onion/10.1038/leu.2014.111 C4169772!4169772!24646888     free     free     free       Leukemia 2014 ; 28 (10): 2040-8 Nephropedia Template TP {{tp|p=24646888|t=2014. Structural basis of Ets1 activation by Runx1 |pdf=|usr=}}{{24646888}} gab.com Text Structural basis of Ets1 activation by Runx1 JO: Leukemia http://www.kidney.de/pget.php?&tw=1&pmid=24646888 #FOAvip Runx1 is required for definitive hematopoiesis and is well-known for its frequent chromosomal translocations and point mutations in leukemia. Runx1 regulates a variety of genes via Ets1 activation on an Ets1?Runx1 composite DNA sequence. The structural basis of such regulation remains unresolved. To address this problem, we determined the crystal structure of the ternary complex containing Runx11-242 and Ets1296-441 bound to T cell receptor alpha (TCR?) enhancer DNA. In the crystal, an Ets1-interacting domain of Runx1 is bound to the Ets1 DNA-binding domain and displaced an entire autoinhibitory module of Ets1, revealing a novel mechanism of Ets1 activation. The DNA binding and transcriptional studies with a variety of structure-guided Runx1 mutants confirmed a critical role of direct Ets1?Runx1 interaction in Ets1 activation. More importantly, the discovered mechanism provides a plausible explanation for how the Ets1?Runx1 interaction effectively activates not only a wild-type Ets1, but also a highly inhibited phosphorylated form of Ets1. Twit Text FOAVip Structural basis of Ets1 activation by Runx1 ????Leukemia http://www.kidney.de/pget.php?&tw=1&pmid=24646888 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24646888 #FOAvip English Wikipedia <ref>{{Cite pmid|24646888}}</ref> Structural basis of Ets1 activation by Runx1 #MMPMID24646888 Shrivastava T; Mino K; Babayeva ND; I.Baranovskaya O; Rizzino A; Tahirov TH Leukemia 2014[Oct]; 28 (10): 2040-8 PMID24646888show ga Runx1 is required for definitive hematopoiesis and is well-known for its frequent chromosomal translocations and point mutations in leukemia. Runx1 regulates a variety of genes via Ets1 activation on an Ets1?Runx1 composite DNA sequence. The structural basis of such regulation remains unresolved. To address this problem, we determined the crystal structure of the ternary complex containing Runx11-242 and Ets1296-441 bound to T cell receptor alpha (TCR?) enhancer DNA. In the crystal, an Ets1-interacting domain of Runx1 is bound to the Ets1 DNA-binding domain and displaced an entire autoinhibitory module of Ets1, revealing a novel mechanism of Ets1 activation. The DNA binding and transcriptional studies with a variety of structure-guided Runx1 mutants confirmed a critical role of direct Ets1?Runx1 interaction in Ets1 activation. More importantly, the discovered mechanism provides a plausible explanation for how the Ets1?Runx1 interaction effectively activates not only a wild-type Ets1, but also a highly inhibited phosphorylated form of Ets1. äStructural basis of Ets1 activation by Runx1 (epmc).pdf DeepDyve Pubget Overpricing