A structural basis for the unique binding features of the human vitamin D-binding protein.

Article Details

Citation

Verboven C, Rabijns A, De Maeyer M, Van Baelen H, Bouillon R, De Ranter C

A structural basis for the unique binding features of the human vitamin D-binding protein.

Nat Struct Biol. 2002 Feb;9(2):131-6.

PubMed ID
11799400 [ View in PubMed
]
Abstract

The human serum vitamin D-binding protein (DBP) has many physiologically important functions, ranging from transporting vitamin D3 metabolites, binding and sequestering globular actin and binding fatty acids to functioning in the immune system. Here we report the 2.3 A crystal structure of DBP in complex with 25-hydroxyvitamin D3, a vitamin D3 metabolite, which reveals the vitamin D-binding site in the N-terminal part of domain I. To more explicitly explore this, we also studied the structure of DBP in complex with a vitamin D3 analog. Comparisons with the structure of human serum albumin, another family member, reveal a similar topology but also significant differences in overall, as well as local, folding. These observed structural differences explain the unique vitamin D3-binding property of DBP.

DrugBank Data that Cites this Article

Drug Carriers
DrugCarrierKindOrganismPharmacological ActionActions
AlfacalcidolVitamin D-binding proteinProteinHumans
Unknown
Substrate
Details
CholecalciferolVitamin D-binding proteinProteinHumans
No
Not AvailableDetails
Polypeptides
NameUniProt ID
Vitamin D-binding proteinP02774Details