1MD0
CRYSTAL STRUCTURE OF AN INHIBITED FRAGMENT OF Ets-1
Summary for 1MD0
| Entry DOI | 10.2210/pdb1md0/pdb |
| Related | 1K79 |
| Descriptor | C-ets-1 protein (2 entities in total) |
| Functional Keywords | autoinhibition, transcription factor, transcription |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Nucleus: P27577 |
| Total number of polymer chains | 2 |
| Total formula weight | 32731.41 |
| Authors | Garvie, C.W.,Pufall, M.A.,Graves, B.J.,Wolberger, C. (deposition date: 2002-08-06, release date: 2002-12-11, Last modification date: 2024-02-14) |
| Primary citation | Garvie, C.W.,Pufall, M.A.,Graves, B.J.,Wolberger, C. Structural Analysis of the Autoinhibition of Ets-1 and Its Role in Protein Partnerships J.Biol.Chem., 277:45529-45536, 2002 Cited by PubMed Abstract: 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). PubMed: 12221090DOI: 10.1074/jbc.M206327200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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