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Conformational Change
(Received for publication, July 2, 1996, and in revised form, October 4, 1996)
§
,
,
and§
From the Structurally diverse peroxisome proliferators and
related compounds that have been demonstrated to induce the
ligand-dependent transcriptional activation function of
mouse peroxisome proliferator-activated receptor 
College of Pharmacy and § Program
in Molecular and Cellular Biology, Oregon State University,
Corvallis, Oregon 97331
(mPPAR) in
transfection experiments were tested for the ability to induce
conformational changes within mPPAR in vitro. WY-14,643,
5,8,11,14-eicosatetraynoic acid, LY-171883, and clofibric acid all
directly induced mPPAR conformational changes as evidenced by a
differential protease sensitivity assay. Carboxyl-terminal truncation
mutagenesis of mPPAR differentially affected the ability of these
ligands to induce conformational changes suggesting that PPAR ligands
may make distinct contacts with the receptor. Direct interaction of
peroxisome proliferators and related compounds with, and the resulting
conformational alteration(s) in, mPPAR may facilitate interaction of
the receptor with transcriptional intermediary factors and/or the
general transcription machinery and, thus, may underlie the molecular
basis of ligand-dependent transcriptional activation
mediated by mPPAR.
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