2jv3
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Ets-1 PNT domain (29-138) NMR structure ensemble
OverviewOverview
The Pointed (PNT) domain and an adjacent mitogen-activated protein (MAP), kinase phosphorylation site are defined by sequence conservation among a, subset of ets transcription factors and are implicated in two regulatory, strategies, protein interactions and posttranslational modifications, respectively. By using NMR, we have determined the structure of a, 110-residue fragment of murine Ets-1 that includes the PNT domain and MAP, kinase site. The Ets-1 PNT domain forms a monomeric five-helix bundle. The, architecture is distinct from that of any known DNA- or protein-binding, module, including the helix-loop-helix fold proposed for the PNT domain of, the ets protein TEL. The MAP kinase site is in a highly flexible region of, both the unphosphorylated and phosphorylated forms of the Ets-1 fragment., Phosphorylation alters neither the structure nor monomeric state of the, PNT domain. These results suggest that the Ets-1 PNT domain functions in, heterotypic protein interactions and support the possibility that target, recognition is coupled to structuring of the MAP kinase site.
About this StructureAbout this Structure
2JV3 is a Single protein structure of sequence from Mus musculus. This structure superseeds the now removed PDB entry 1BQV. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site., Slupsky CM, Gentile LN, Donaldson LW, Mackereth CD, Seidel JJ, Graves BJ, McIntosh LP, Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12129-34. PMID:9770451
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