1md0

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[[Image:1md0.gif|left|200px]]
[[Image:1md0.gif|left|200px]]
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{{Structure
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|GENE= ETS-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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{{STRUCTURE_1md0| PDB=1md0 | SCENE= }}
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|RELATEDENTRY=[[1k79|1K79]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1md0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1md0 OCA], [http://www.ebi.ac.uk/pdbsum/1md0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1md0 RCSB]</span>
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'''CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1'''
'''CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1'''
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[[Category: Pufall, M A.]]
[[Category: Pufall, M A.]]
[[Category: Wolberger, C.]]
[[Category: Wolberger, C.]]
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[[Category: autoinhibition]]
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[[Category: Autoinhibition]]
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[[Category: transcription factor]]
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[[Category: Transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:53:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:14:37 2008''
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Revision as of 21:53, 2 May 2008

Template:STRUCTURE 1md0

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 Page seeded by OCA on Sat May 3 00:53:58 2008

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