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Biophys J, January 1999, p. 188-197, Vol. 76, No. 1
Departments of Chemistry and Physics, Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801 USA
Retinoic acid receptor (RAR) is a ligand-dependent
transcription factor that regulates the expression of genes involved in cell growth, differentiation, and development. Binding of the retinoic
acid hormone to RAR is accompanied by conformational changes in the
protein which induce transactivation or transrepression of the target
genes. In this paper we present a study of the hormone binding/unbinding process in order to clarify the role of some of the
amino acid contacts and identify possible pathways of the all-trans retinoic acid binding/unbinding to/from human
retinoic acid receptor (hRAR)-
. Three possible pathways were
explored using steered molecular dynamics simulations. Unbinding was
induced on a time scale of 1 ns by applying external forces to the
hormone. The simulations suggest that the hormone may employ one
pathway for binding and an alternative "back door" pathway for unbinding.
Biophys J, January 1999, p. 188-197, Vol. 76, No. 1
© 1999 by the Biophysical Society 0006-3495/99/01/188/10 $2.00
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