1md0: Difference between revisions

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[[Image:1md0.gif|left|200px]]
{{Seed}}
[[Image:1md0.png|left|200px]]


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{{STRUCTURE_1md0|  PDB=1md0  |  SCENE=  }}  
{{STRUCTURE_1md0|  PDB=1md0  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1'''
===CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1===




==Overview==
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The DNA-binding activity of the eukaryotic transcription factor Ets-1 (E26 avian erythroblastosis virus oncogene-E twenty-six) is negatively regulated by inhibitory regions that flank the ETS domain. Based on the results of solution studies, these N- and C-terminal inhibitory regions have been proposed to pack against the ETS domain and form an autoinhibitory module whose N terminus partially unfolds upon binding of Ets-1 to DNA. Mutations that disrupt autoinhibition of DNA binding also cause a structural change in the inhibitory region. We report here a crystallographic study of fragments of Ets-1 that provide structural details of the inhibitory module and the structural transition that accompanies DNA binding. The structures of free and DNA-bound Ets-1 fragments containing the ETS domain and the inhibitory regions confirm that the N-terminal inhibitory region contains two alpha-helices one of which unfolds upon Ets-1 binding to DNA. The observations from the crystal structure, coupled with mutagenesis experiments, allow us to propose a model for the inhibited form of Ets-1 and lend insight into the flexible interaction between Ets-1 and the acute myeloid leukemia 1 protein, AML1 (RUNX1).
The line below this paragraph, {{ABSTRACT_PUBMED_12221090}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12221090 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12221090}}


==About this Structure==
==About this Structure==
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[[Category: Autoinhibition]]
[[Category: Autoinhibition]]
[[Category: Transcription factor]]
[[Category: Transcription factor]]
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