1OJ5

Crystal structure of the Nco-A1 PAS-B domain bound to the STAT6 transactivation domain LXXLL motif

1OJ5 の概要

• エントリーDOI: 10.2210/pdb1oj5/pdb
• 関連するPDBエントリー: 1K74 1K7L 2PRG
• 分子名称: STEROID RECEPTOR COACTIVATOR 1A, SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 6, IODIDE ION, ... (4 entities in total)
• 機能のキーワード: transcriptional coactivator, complex, lxxll motif, transcriptional regulation, stat6, pas domain, il-4 stat
• 由来する生物種: MUS MUSCULUS (MOUSE); 詳細
• 細胞内の位置: Cytoplasm: P42226
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17057.16

構造登録者

Razeto, A.,Ramakrishnan, V.,Giller, K.,Lakomek, N.,Carlomagno, T.,Griesinger, C.,Lodrini, M.,Litterst, C.M.,Pftizner, E.,Becker, S. (登録日: 2003-07-02, 公開日: 2004-02-12, 最終更新日: 2024-05-08)

主引用文献

Razeto, A.,Ramakrishnan, V.,Litterst, C.M.,Giller, K.,Griesinger, C.,Carlomagno, T.,Lakomek, N.,Heimburg, T.,Lodrini, M.,Pfitzner, E.,Becker, S.
Structure of the Ncoa-1/Src-1 Pas-B Domain Bound to the Lxxll Motif of the Stat6 Transactivation Domain
J.Mol.Biol., 336:319-, 2004

PubMed Abstract: Signal transducer and activator of transcription 6 (STAT6) regulates transcriptional activation in response to interleukin-4 (IL-4) by direct interaction with coactivators. The CREB-binding protein (p300/CBP) and the nuclear coactivator 1 (NCoA-1), a member of the p160/steroid receptor coactivator family, bind independently to specific regions of the STAT6 transactivation domain and act as coactivators. The interaction between STAT6 and NCoA-1 is mediated by an LXXLL motif in the transactivation domain of STAT6. To define the mechanism of coactivator recognition, we determined the crystal structure of the NCoA-1 PAS-B domain in complex with the STAT6 LXXLL motif. The amphipathic, alpha-helical STAT6 LXXLL motif binds mostly through specific hydrophobic interactions to NCoA-1. A single amino acid of the NCoA-1 PAS-B domain establishes hydrophilic interactions with the STAT6 peptide. STAT6 interacts only with the PAS-B domain of NCoA-1 but not with the homologous regions of NCoA-2 and NCoA-3. The residues involved in binding the STAT6 peptide are strongly conserved between the different NCoA family members. Therefore surface complementarity between the hydrophobic faces of the STAT6 fragment and of the NCoA-1 PAS-B domain almost exclusively defines the binding specificity between the two proteins.

PubMed: 14757047
DOI: 10.1016/J.JMB.2003.12.057

実験手法

X-RAY DIFFRACTION (2.21 Å)