![]() Y Chen, L Lin, I Agyekum, X Zhang, KS Ange, Y Yu. Taken together, these results indicate that subtle structural changes in a nuclear receptor DBD can exert long-range functional effects on the LBD of a receptor, and significantly impact transcriptional regulation. Structural analysis of heparin-derived 3-O-sulfated tetrasaccharides: antithrombin binding site variants. Moreover, we find that altering the Ftz-F1 helix positioning eliminates the enhancement of LRH-1-mediated transcription by the coactivator GRIP1, an action that is associated primarily with the distantly located ligand-binding domain (LBD). Mutations expected to disrupt the positioning of the Ftz-F1 helix do not eliminate DNA binding but reduce the transcriptional activity of full-length LRH-1 significantly. ![]() Isaac Agyekum1, Lauren Pepi1, Yanlei Yu2, Junhui Li3. We show that the unique Ftz-F1 domain folds into a novel helix that packs against the DBD but does not contact DNA. Structural elucidation of fucosylated chondroitin sulfates from sea cucumber using FTICR-MS/MS. Here, we present the 2.2A resolution crystal structure of the hLRH-1 DBD in complex with duplex DNA, and elucidate the sequence-specific DNA contacts essential for the ability of LRH-1 to bind to DNA as a monomer. The Binding of Isaac is a randomly generated action RPG shooter with heavy Rogue-like elements. ![]() The DNA-binding domain (DBD) of the human liver receptor homologue-1 (hLRH-1), which controls genes central to development and metabolic homeostasis, interacts with monomeric DNA response elements and contains an Ftz-F1 motif that is unique to the NR5A nuclear receptor subfamily. The DNA-binding and ligand-binding functions of nuclear receptors are localized to independent domains separated by a flexible hinge. ![]()
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