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Related Experiment Videos

The transthyretin-retinol-binding protein complex.

H L Monaco1

  • 1Biocrystallography Laboratory, Department of Science and Technology, University of Verona, Strada Le Grazie 15, 37134 Verona, Italy.

Biochimica Et Biophysica Acta
|November 4, 2000
PubMed
Summary

Transthyretin (TTR) and retinol-binding protein (RBP) form a complex to prevent RBP filtration in kidneys. This study reviews the physiological significance, structure, and models of this macromolecular interaction.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • Transthyretin (TTR) transports thyroxine and binds retinol-binding protein (RBP).
  • Retinol-binding protein (RBP) is the specific carrier for vitamin A.
  • TTR and RBP form a macromolecular complex under physiological conditions.

Purpose of the Study:

  • To discuss the physiological significance of the TTR-RBP complex formation.
  • To describe the three-dimensional structure of TTR and RBP.
  • To compare available X-ray models of the complex and review supporting evidence.

Main Methods:

  • Review of physiological roles of TTR-RBP complex.
  • Description of TTR and RBP protein structures.
  • Analysis and comparison of X-ray crystallographic models.

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  • Review of non-crystallographic evidence.

    • Main Results:

    • The TTR-RBP complex is believed to prevent glomerular filtration of RBP in the kidneys.
    • Detailed structural information of TTR and RBP is presented.
    • Two distinct X-ray models of the complex are discussed and compared.

    Conclusions:

    • Complex formation between TTR and RBP plays a crucial role in renal physiology.
    • Structural insights support the proposed function of the TTR-RBP complex.
    • Further evidence supports the validity of the presented structural models.