tailieunhanh - Báo cáo khoa học: Evidence for b-lactoglobulin involvement in vitamin D transport in vivo – role of the c-turn (Leu-Pro-Met) of b-lactoglobulin in vitamin D binding

b-lactoglobulin (LG) is a major bovine milk protein, containing a central calyx and a second exosite beyond the calyx to bind vitamin D; however, the biological function of LG in transporting vitamin D remains elusive. Crystallographic findings from our previous study showed the exosite to be located at the pocket between the a-helix and b-strand I. | ỊFEBS Journal Evidence for b-lactoglobulin involvement in vitamin D transport in vivo - role of the c-turn Leu-Pro-Met of b-lactoglobulin in vitamin D binding Ming Chi Yang1 Nai Chi Chen1 Chun-Jung Chen2 3 Chin Yun Wu1 and Simon J. T. Mao1 4 1 Department and College of BiologicalScience and Technology NationalChiao Tung University Taiwan 2 Life Science Group Research Division NationalSynchrotron Radiation Research Center Taiwan 3 Department of Physics NationalTsing Hua University Taiwan 4 Department of Biotechnology and Bioinformatics Asia University Taichung Taiwan Keywords b-lactoglobulin monoclonalantibody site-directed mutagenesis vitamin D binding vitamin D transport and uptake Correspondence S. J. T. Mao Department of Biological Science and Technology College of BiologicalScience and Technology National Chiao Tung University 75 Po-Ai Street Hsinchu 30050 Taiwan Fax 886 3 572 9288 Tel 886 3 571 2121 ext. 56948 E-mail mao1010@ Received 9 December 2008 revised 3 February 2009 accepted 6 February 2009 doi b-lactoglobulin LG is a major bovine milk protein containing a central calyx and a second exosite beyond the calyx to bind vitamin D however the biological function of LG in transporting vitamin D remains elusive. Crystallographic findings from our previous study showed the exosite to be located at the pocket between the a-helix and b-strand I. In the present study using site-directed mutagenesis we demonstrate that residues Leu143 Pro144 and Met145 in the y-turn loop play a crucial role in the binding. Further evidence is provided by the ability of vitamin D3 to block the binding of a specific mAb in the y-turn loop. Using the mouse n 95 as an animal model we initially demonstrated that LG is a major fraction of milk proteins responsible for uptake of vitamin D. Most interestingly dosing mice with LG supplemented with vitamin D3 revealed that native LG containing two binding sites gave a saturated concentration of .

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