Molecular Recognition in Vitamin D-Binding Protein (44020)

Ray, Rahul

Bioorganic and Protein Chemistry, Vitamin D Laboratory, and Department of Physiology, Boston University School of Medicine, Boston, Massachusetts 02118

¹To whom requests for reprints should be addressed at Bioorganic/Protein Chemistry, Vitamin D Laboratory, and Department of Physiology, Boston University School of Medicine, Boston, MA 02118.

Parts of the work discussed in this review were made possible by grants (RO1 DK 44337 and 47418) from the National Institute of Diabetes, Digestive, and Kidney Diseases.

Proceedings of the Society for Experimental Biology & Medicine 212(4):p 305-312, September 1996.

Vitamin D-binding protein (DBP) or group-specific component (Gc) is a relatively abundant serum protein with multiple functions, the majority of which are initiated by the highly specific recognition and binding of a ligand by this protein. During the past decade and a half, several structure-functional studies have been carried out to shed light on the physiological significance of the multiple functions of DBP. Results of these studies are discussed.