1bsx
From Proteopedia
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STRUCTURE AND SPECIFICITY OF NUCLEAR RECEPTOR-COACTIVATOR INTERACTIONS
Overview
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 ... [(full description)]
About this Structure
1BSX is a [Single protein] structure of sequence from [Homo sapiens] with T3 as [ligand]. Structure known Active Sites: A and B. Full crystallographic information is available from [OCA].
Reference
Structure and specificity of nuclear receptor-coactivator interactions., Darimont BD, Wagner RL, Apriletti JW, Stallcup MR, Kushner PJ, Baxter JD, Fletterick RJ, Yamamoto KR, Genes Dev. 1998 Nov 1;12(21):3343-56. PMID:9808622
Page seeded by OCA on Tue Oct 30 14:57:14 2007
