4NUF
Crystal Structure of SHP/EID1
Summary for 4NUF
| Entry DOI | 10.2210/pdb4nuf/pdb |
| Related PRD ID | PRD_900001 |
| Descriptor | 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) |
| Functional Keywords | protein-peptide complex, peptide mimicking protein helix, sandwich fold, transport protein, transcription |
| Biological source | Escherichia coli O104:H4 More |
| Total number of polymer chains | 2 |
| Total formula weight | 66345.65 |
| Authors | Zhi, X.,Zhou, X.E.,He, Y.,Zechner, C.,Suino-Powell, K.M.,Kliewer, S.A.,Melcher, K.,Mangelsdorf, D.J.,Xu, H.E. (deposition date: 2013-12-03, release date: 2014-01-29, Last modification date: 2024-02-28) |
| Primary citation | 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 Cited by 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: 24379397DOI: 10.1073/pnas.1322827111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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