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Retinoid-binding proteins: structural determinants important for function

M E Newcomer1

  • 1Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, USA.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|February 1, 1995
PubMed
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This review details how proteins transport Vitamin A and its metabolites. Structural analysis reveals distinct binding mechanisms for extracellular and intracellular retinoid-binding proteins.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Biologically active retinoids, including Vitamin A and retinol, are essential for various physiological functions.
  • Their transport and function rely on interactions with specific extracellular, intracellular, and nuclear proteins.
  • Understanding these interactions is crucial for comprehending retinoid metabolism and signaling.

Purpose of the Study:

  • To review the distinct mechanisms by which extracellular and intracellular proteins recognize and bind retinoids.
  • To elucidate the structural basis underlying these retinoid-protein interactions.
  • To provide insights into the structure-function relationships of retinoid transport proteins.

Main Methods:

  • X-ray crystallography was employed to study the structures of key retinoid-binding proteins.

Related Experiment Videos

  • Comparative analysis of structural motifs in extracellular and intracellular retinoid-binding proteins.
  • Detailed examination of the binding cavities and ligand interactions.

    • Main Results:

    • Extracellular proteins, such as serum retinol-binding protein, exhibit a "hand-in-glove" fit within deep, hydrophobic binding cavities.
    • Intracellular proteins, like cellular retinol-binding proteins I and II, encapsulate retinoids within internal aqueous cavities.
    • Distinct structural motifs correlate with specific retinoid recognition and binding strategies.

    Conclusions:

    • Protein structure dictates the mechanism of retinoid recognition and binding.
    • Extracellular and intracellular retinoid-binding proteins employ fundamentally different structural strategies for ligand interaction.
    • This structural diversity facilitates the precise transport and functional regulation of retinoids within biological systems.