1mdm
From Proteopedia
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INHIBITED FRAGMENT OF ETS-1 AND PAIRED DOMAIN OF PAX5 BOUND TO DNA
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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).
Disease
Known disease associated with this structure: Lymphoplasmacytoid lymphoma OMIM:[167414]
About this Structure
1MDM is a Protein complex structure of sequences from Homo sapiens and 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 Mon Nov 12 18:10:14 2007
