1zh7

<table><tr><td colspan='2'>[[1zh7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZH7 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zh7 OCA], [https://pdbe.org/1zh7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zh7 RCSB], [https://www.ebi.ac.uk/pdbsum/1zh7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zh7 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/NR5A2_MOUSE NR5A2_MOUSE]] Binds to promoters containing the sequence element 5'-AACGACCGACCTTGAG-3'. Plays a role in the regulation of gene expression in liver and pancreas. May play a role in embryonic development (By similarity). [[https://www.uniprot.org/uniprot/NR0B2_RAT NR0B2_RAT]] Acts as a transcriptional regulator. Acts as a negative regulator of receptor-dependent signaling pathways. Specifically inhibits transactivation of the nuclear receptor with whom it interacts. Inhibits transcriptional activity of NEUROD1 on E-box-containing promoter by interfering with the coactivation function of the p300/CBP-mediated trancription complex for NEUROD1.

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== Publication Abstract from PubMed ==

The functional interaction between the orphan nuclear receptors small heterodimer partner (SHP) and liver receptor homolog 1 (LRH-1), where SHP binds to LRH-1 and represses its constitutive transcriptional activity, is crucial for regulating genes involved in cholesterol homeostasis. Here, we report structural and biochemical analyses of the LRH-1/SHP interaction. The crystal structure and modeling studies of the LRH-1 ligand-binding domain bound to either of the two LXXLL-related motifs of SHP show that the receptor undergoes conformational changes to accommodate the SHP docking and reveal key residues that determine the potency and selectivity of SHP binding. Through a combination of mutagenesis and binding studies, we demonstrate that only the second SHP LXXLL motif is required for repressing LRH-1, and this motif displays a strong preference for binding to LRH-1 over the closely related receptor steroidogeneic factor 1 (SF-1). Structural comparisons indicate that this binding selectivity is determined by residues flanking the core LXXLL motifs. These results establish a structural model for understanding how SHP interacts with LRH-1 to regulate cholesterol homeostasis and provide new insights into how nuclear receptor/coregulator selectivity is achieved.

Structural and biochemical basis for selective repression of the orphan nuclear receptor liver receptor homolog 1 by small heterodimer partner.,Li Y, Choi M, Suino K, Kovach A, Daugherty J, Kliewer SA, Xu HE Proc Natl Acad Sci U S A. 2005 Jul 5;102(27):9505-10. Epub 2005 Jun 23. PMID:15976031<ref>PMID:15976031</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Buffalo rat]]

[[Category: Lk3 transgenic mice]]

[[Category: Choi, M]]

[[Category: Daugherty, J]]

[[Category: Kliewer, S A]]

[[Category: Kovach, A]]

[[Category: Li, Y]]

[[Category: Suino, K]]

[[Category: Xu, H E]]

[[Category: Transcription]]