4NUF

Crystal Structure of SHP/EID1

4NUF の概要

• エントリーDOI: 10.2210/pdb4nuf/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose ABC transporter periplasmic protein, Nuclear receptor subfamily 0 group B member 2 chimeric construct, EID1 peptide, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: protein-peptide complex, peptide mimicking protein helix, sandwich fold, transport protein, transcription
• 由来する生物種: Escherichia coli O104:H4; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66345.65

構造登録者

Zhi, X.,Zhou, X.E.,He, Y.,Zechner, C.,Suino-Powell, K.M.,Kliewer, S.A.,Melcher, K.,Mangelsdorf, D.J.,Xu, H.E. (登録日: 2013-12-03, 公開日: 2014-01-29, 最終更新日: 2024-02-28)

主引用文献

Zhi, X.,Zhou, X.E.,He, Y.,Zechner, C.,Suino-Powell, K.M.,Kliewer, S.A.,Melcher, K.,Mangelsdorf, D.J.,Xu, H.E.
Structural insights into gene repression by the orphan nuclear receptor SHP.
Proc.Natl.Acad.Sci.USA, 111:839-844, 2014

PubMed Abstract: Small heterodimer partner (SHP) is an orphan nuclear receptor that functions as a transcriptional repressor to regulate bile acid and cholesterol homeostasis. Although the precise mechanism whereby SHP represses transcription is not known, E1A-like inhibitor of differentiation (EID1) was isolated as a SHP-interacting protein and implicated in SHP repression. Here we present the crystal structure of SHP in complex with EID1, which reveals an unexpected EID1-binding site on SHP. Unlike the classical cofactor-binding site near the C-terminal helix H12, the EID1-binding site is located at the N terminus of the receptor, where EID1 mimics helix H1 of the nuclear receptor ligand-binding domain. The residues composing the SHP-EID1 interface are highly conserved. Their mutation diminishes SHP-EID1 interactions and affects SHP repressor activity. Together, these results provide important structural insights into SHP cofactor recruitment and repressor function and reveal a conserved protein interface that is likely to have broad implications for transcriptional repression by orphan nuclear receptors.

PubMed: 24379397
DOI: 10.1073/pnas.1322827111

実験手法

X-RAY DIFFRACTION (2.8 Å)