1md0
From Proteopedia
(New page: 200px<br /><applet load="1md0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1md0, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1md0.gif|left|200px]]<br /><applet load="1md0" size=" | + | [[Image:1md0.gif|left|200px]]<br /><applet load="1md0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1md0, resolution 2.00Å" /> | caption="1md0, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1'''<br /> | '''CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The DNA-binding activity of the eukaryotic transcription factor Ets-1 (E26 | + | 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). |
==About this Structure== | ==About this Structure== | ||
| - | 1MD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1MD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MD0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Garvie, C | + | [[Category: Garvie, C W.]] |
| - | [[Category: Graves, B | + | [[Category: Graves, B J.]] |
| - | [[Category: Pufall, M | + | [[Category: Pufall, M A.]] |
[[Category: Wolberger, C.]] | [[Category: Wolberger, C.]] | ||
[[Category: autoinhibition]] | [[Category: autoinhibition]] | ||
[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:00 2008'' |
Revision as of 11:54, 21 February 2008
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CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1
Overview
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).
About this Structure
1MD0 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships., Garvie CW, Pufall MA, Graves BJ, Wolberger C, J Biol Chem. 2002 Nov 22;277(47):45529-36. Epub 2002 Sep 6. PMID:12221090
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