BIOL 3051 Chapter Notes - Chapter 9.1: Histone Acetyltransferase, Af2, Alpha Helix
24 Apr 2020
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Ligand binding domains of nrs are conserved: 3ds structure made of 11-12 alpha helices very specific fold, alpha helices have hydrophobic domain, af2 helix at end that moves when ligand is present. Ligand binding pocket: ligand binding pocket differs, binding pocket is small for dhr38 less accommodating, lots of drugs bind to pxr b/c large pocket that accommodates multiple structures. Role of ligand: ligands bind & promote activation of gene transcription. Af2 helix: molecular switch cornr box & nr box: when no ligand bound, lbd is empty. Af2 is in conformation that binds with corepressor. Af2 interacts with lxxxixxxl/i sequence: when ligand present, af2 moves & exposes new surface that interacts w/coactivators. Af2 interacts with lxxll motif recruits other proteins for gene transcription: agonist stabilizes receptors coactivator bound state, antagonist stabilize receptors co-repressor bound state. In open conformation hat (histone acetyltransferase) histones acetylated unwraps dna more available for gene expression.
