1j7e

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spinqualitylabelsall models 1j7e, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

A Structural Basis for the Unique Binding Features of the Human Vitamin D-binding Protein

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known disease associated with this structure: Graves disease, susceptibility to, 3 OMIM:[139200]

About this Structure

1J7E is a Single protein structure of sequence from Homo sapiens with JY and OLA as ligands. Full crystallographic information is available from OCA.

Reference

A structural basis for the unique binding features of the human vitamin D-binding protein., Verboven C, Rabijns A, De Maeyer M, Van Baelen H, Bouillon R, De Ranter C, Nat Struct Biol. 2002 Feb;9(2):131-6. PMID:11799400

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