1SXE

The solution structure of the Pointed (PNT) domain from the transcrition factor Erg

1SXE の概要

• エントリーDOI: 10.2210/pdb1sxe/pdb
• NMR情報: BMRB: 5399
• 分子名称: Transcriptional regulator ERG (1 entity in total)
• 機能のキーワード: alpha helical, transcription, signaling protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P11308
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11395.99

構造登録者

Mackereth, C.D.,Schaerpf, M.,Gentile, L.N.,MacIntosh, S.E.,Slupsky, C.M.,McIntosh, L.P. (登録日: 2004-03-30, 公開日: 2004-09-21, 最終更新日: 2024-05-22)

主引用文献

Mackereth, C.D.,Schaerpf, M.,Gentile, L.N.,MacIntosh, S.E.,Slupsky, C.M.,McIntosh, L.P.
Diversity in Structure and Function of the Ets Family PNT Domains.
J.Mol.Biol., 342:1249-1264, 2004

PubMed Abstract: The PNT (or Pointed) domain, present within a subset of the Ets family of transcription factors, is structurally related to the larger group of SAM domains through a common tertiary arrangement of four alpha-helices. Previous studies have shown that, in contrast to the PNT domain from Tel, this domain from Ets-1 contains an additional N-terminal helix integral to its folded structure. To further investigate the structural plasticity of the PNT domain, we have used NMR spectroscopy to characterize this domain from two additional Ets proteins, Erg and GABPalpha. These studies both define the conserved and variable features of the PNT domain, and demonstrate that the additional N-terminal helix is also present in GABPalpha, but not Erg. In contrast to Tel and Yan, which self-associate to form insoluble polymers, we also show that the isolated PNT domains from Ets-1, Ets-2, Erg, Fli-1, GABPalpha, and Pnt-P2 are monomeric in solution. Furthermore, these soluble PNT domains do not associate in any pair-wise combination. Thus these latter Ets family PNT domains likely mediate interactions with additional components of the cellular signaling or transcriptional machinery.

PubMed: 15351649
DOI: 10.1016/j.jmb.2004.07.094

実験手法

SOLUTION NMR