1J78

Crystallographic analysis of the human vitamin D binding protein

Summary for 1J78

• Entry DOI: 10.2210/pdb1j78/pdb
• Related: 1J7E
• Descriptor: vitamin D binding protein, OLEIC ACID, 3-{2-[1-(5-HYDROXY-1,5-DIMETHYL-HEXYL)-7A-METHYL-OCTAHYDRO-INDEN-4-YLIDENE]-ETHYLIDENE}-4-METHYLENE-CYCLOHEXANOL, ... (4 entities in total)
• Functional Keywords: plasma protein, vitamin d binding, actin binding, fatty acid binding, gc-globulin, group-specific component, transport, ligand binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted : P02774
• Total number of polymer chains: 2
• Total formula weight: 103802.60

Authors

Verboven, C.,Rabijns, A.,De Maeyer, M.,Van Baelen, H.,Bouillon, R.,De Ranter, C. (deposition date: 2001-05-16, release date: 2002-02-06, Last modification date: 2024-10-30)

Primary 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., 9:131-136, 2002

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.

PubMed: 11799400
DOI: 10.1038/nsb754

Experimental method

X-RAY DIFFRACTION (2.31 Å)