1BSX

STRUCTURE AND SPECIFICITY OF NUCLEAR RECEPTOR-COACTIVATOR INTERACTIONS

1BSX の概要

• エントリーDOI: 10.2210/pdb1bsx/pdb
• 分子名称: PROTEIN (THYROID HORMONE RECEPTOR BETA), PROTEIN (GRIP1), 3,5,3'TRIIODOTHYRONINE (3 entities in total)
• 機能のキーワード: nuclear receptors, coactivators, grip1, specificity interaction site, hormone-growth factor complex, hormone/growth factor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P10828
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63139.41

構造登録者

Wagner, R.L.,Darimont, B.D.,Apriletti, J.W.,Stallcup, M.R.,Kushner, P.J.,Baxter, J.D.,Fletterick, R.J.,Yamamoto, K.R. (登録日: 1998-08-31, 公開日: 1999-08-26, 最終更新日: 2024-04-03)

主引用文献

Darimont, B.D.,Wagner, R.L.,Apriletti, J.W.,Stallcup, M.R.,Kushner, P.J.,Baxter, J.D.,Fletterick, R.J.,Yamamoto, K.R.
Structure and specificity of nuclear receptor-coactivator interactions.
Genes Dev., 12:3343-3356, 1998

PubMed Abstract: Combinatorial regulation of transcription implies flexible yet precise assembly of multiprotein regulatory complexes in response to signals. Biochemical and crystallographic analyses revealed that hormone binding leads to the formation of a hydrophobic groove within the ligand binding domain (LBD) of the thyroid hormone receptor that interacts with an LxxLL motif-containing alpha-helix from GRIP1, a coactivator. Residues immediately adjacent to the motif modulate the affinity of the interaction; the motif and the adjacent sequences are employed to different extents in binding to different receptors. Such interactions of amphipathic alpha-helices with hydrophobic grooves define protein interfaces in other regulatory complexes as well. We suggest that these common structural elements impart flexibility to combinatorial regulation, whereas side chains at the interface impart specificity.

PubMed: 9808622

実験手法

X-RAY DIFFRACTION (3.7 Å)