1J78

Crystallographic analysis of the human vitamin D binding protein

1J78 の概要

• エントリーDOI: 10.2210/pdb1j78/pdb
• 関連するPDBエントリー: 1J7E
• 分子名称: 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)
• 機能のキーワード: plasma protein, vitamin d binding, actin binding, fatty acid binding, gc-globulin, group-specific component, transport, ligand binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted : P02774
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103802.60

構造登録者

Verboven, C.,Rabijns, A.,De Maeyer, M.,Van Baelen, H.,Bouillon, R.,De Ranter, C. (登録日: 2001-05-16, 公開日: 2002-02-06, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.31 Å)