Retinoid-binding proteins: structural determinants important for function.

M E Newcomer

doi:10.1096/fasebj.9.2.7781925

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PubMed · 7781925

Retinoid-binding proteins: structural determinants important for function.

M E Newcomer

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Abstract

The transport and functions of biologically active naturally occurring retinoids (Vitamin A, retinol, and its metabolites) are mediated by extracellular, intracellular, and nuclear proteins. X-ray crystallographic studies to date on the extra- and intracellular proteins have helped to define distinct protein retinoid recognition mechanisms, each with a characteristic structural motif. The extracellular proteins (serum retinol-binding protein and a retinoic acid-binding protein from rat epididymis) bind retinoids with a hand-in-glove like fit in deep, hydrophobic-binding cavities. The intracellular proteins (cellular retinol-binding proteins types I and II) encapsulate the ligand in an aqueous internal cavity. The details of the mechanisms of retinoid recognition, and how they result as a consequence of the different protein structures, are described in this review.

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Amino Acid Sequence Animals Binding Sites Crystallography, X-Ray Humans Models, Molecular Molecular Sequence Data Protein Conformation Retinol-Binding Proteins Sequence Homology, Amino Acid Tretinoin Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.Review

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M E Newcomer. 1995. Retinoid-binding proteins: structural determinants important for function.. https://doi.org/10.1096/fasebj.9.2.7781925

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