Title : Molecular docking studies on interaction of diverse retinol structures with human alcohol dehydrogenases predict a broad role in retinoid ligand synthesis.

Pub. Date : 1999 Jul 13

PMID : 10407146






4 Functional Relationships(s)
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1 The crystal structures of human ADH1B and ADH4 provide the opportunity to examine their active sites for potential binding to many diverse retinol structures using molecular docking algorithms. Vitamin A alcohol dehydrogenase 4 (class II), pi polypeptide Homo sapiens
2 By these criteria, all-trans-retinol, 4-oxo-retinol, and 4-hydroxy-retinol were successfully docked to both ADH1B and ADH4. Vitamin A alcohol dehydrogenase 4 (class II), pi polypeptide Homo sapiens
3 Furthermore, docking of all retinols was more favorable in the active site of ADH4 rather than ADH1B as measured by force field and contact scores. Vitamin A alcohol dehydrogenase 4 (class II), pi polypeptide Homo sapiens
4 These findings suggest that ADH1B has a limited capacity to metabolize retinols, but that ADH4 is well suited to function in the metabolism of many diverse retinols and is predicted to participate in the synthesis of the active ligands all-trans-retinoic acid, 9-cis-retinoic acid, 3, 4-didehydroretinoic acid, 4-oxo-retinoic acid, and 4-hydroxy-retinoic acid. Vitamin A alcohol dehydrogenase 4 (class II), pi polypeptide Homo sapiens