Title | Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site |
Publication Type | Journal Article |
Year of Publication | 1998 |
Authors | Slupsky, CM, Gentile, LN, Donaldson, LW, Mackereth, CD, Seidel, JJ, Graves, BJ, McIntosh, LP |
Journal | Proceedings of the National Academy of Sciences of the United States of America |
Volume | 95 |
Pagination | 12129-12134 |
Date Published | Oct |
Type of Article | Article |
ISBN Number | 0027-8424 |
Keywords | beta, CHRONIC MYELOMONOCYTIC LEUKEMIA, FUSION, GENE, NMR, OLIGOMERIZATION, TEL, TRANSCRIPTION FACTORS, TRANSLOCATION, TROPONIN-C |
Abstract | 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. |
URL | <Go to ISI>://000076447900013 |
