2jv3
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 supersedes 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 Page seeded by OCA on Sun May 4 09:19:26 2008