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Structure and function of cytoplasmic retinoid binding proteins

  • Ellen Li
Part of the Molecular and Cellular Biochemistry book series (DMCB, volume 29)

Abstract

We examined the ligand protein interactions of two highly homologous cellular retinol binding proteins, CRBP and CRBP-II, and two highly homologous cellular retinoic acid binding proteins, CRABP-I and CRABP-II. While the crystal structures of all four have been determined, nuclear magnetic resonance studies provide a means for observing dynamic aspects of ligand protein interactions of these proteins in solution. The cellular functions of these proteins are less well understood. We have modeled retinoid flux between cytoplasmic retinoid proteins and model membranes and with nuclear receptors. Based on our in vitro studies, we propose that certain retinoids may indirectly influence retinoid signaling by displacing endogenous retinoids from the cytoplasmic proteins to the nuclear receptors. (Mol Cell Biochem 192: 105–108, 1999)

Key words

retinal binding proteins cytoplasmic retinoid proteins 

Abbreviations

CRBP

cellular retinol binding protein

CRABP

cellular retinoic acid binding protein

iLBP

intracellular lipid binding protein

RAR

retinoic acid receptor

RXR

retinoid-X-receptor

NMR

nuclear magnetic resonance

NOESY

nuclear Overhauser effect spectroscopy

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Copyright information

© Springer Science+Business Media Dordrecht 1999

Authors and Affiliations

  • Ellen Li
    • 1
  1. 1.Departments of Medicine, Biochemistry and Molecular BiophysicsWashington University, School of MedicineSt. LouisUSA

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