1prg
From Proteopedia
|
LIGAND BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA
Overview
The peroxisome proliferator-activated receptor-gamma (PPAR-gamma) is a, ligand-dependent transcription factor that is important in adipocyte, differentiation and glucose homeostasis and which depends on interactions, with co-activators, including steroid receptor co-activating factor-1, (SRC-1). Here we present the X-ray crystal structure of the human, apo-PPAR-gamma ligand-binding domain (LBD), at 2.2 A resolution; this, structure reveals a large binding pocket, which may explain the diversity, of ligands for PPAR-gamma. We also describe the ternary complex containing, the PPAR-gamma LBD, the antidiabetic ligand rosiglitazone (BRL49653), and, 88 amino acids of human SRC-1 at 2.3 A resolution. Glutamate and lysine, residues that are highly conserved in LBDs of nuclear receptors form a, 'charge clamp' that contacts backbone atoms of the LXXLL helices of SRC-1., These results, together with the observation that two consecutive LXXLL, motifs of SRC-1 make identical contacts with both subunits of a PPAR-gamma, homodimer, suggest a general mechanism for the assembly of nuclear, receptors with co-activators.
About this Structure
1PRG is a Single protein structure of sequence from Homo sapiens. Structure known Active Sites: LLL and LND. Full crystallographic information is available from OCA.
Reference
Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma., Nolte RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV, Nature. 1998 Sep 10;395(6698):137-43. PMID:9744270
Page seeded by OCA on Mon Nov 5 14:56:41 2007
