1j7e
From Proteopedia
(New page: 200px<br /> <applet load="1j7e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j7e, resolution 2.55Å" /> '''A Structural Basis ...) |
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caption="1j7e, resolution 2.55Å" /> | caption="1j7e, resolution 2.55Å" /> | ||
'''A Structural Basis for the Unique Binding Features of the Human Vitamin D-binding Protein'''<br /> | '''A Structural Basis for the Unique Binding Features of the Human Vitamin D-binding Protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The human serum vitamin D-binding protein (DBP) has many physiologically | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1J7E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with JY and OLA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1J7E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=JY:'>JY</scene> and <scene name='pdbligand=OLA:'>OLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J7E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Baelen, H | + | [[Category: Baelen, H Van.]] |
[[Category: Bouillon, R.]] | [[Category: Bouillon, R.]] | ||
| - | [[Category: Maeyer, M | + | [[Category: Maeyer, M De.]] |
[[Category: Rabijns, A.]] | [[Category: Rabijns, A.]] | ||
| - | [[Category: Ranter, C | + | [[Category: Ranter, C De.]] |
[[Category: Verboven, C.]] | [[Category: Verboven, C.]] | ||
[[Category: JY]] | [[Category: JY]] | ||
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[[Category: vitamin d3 analogue]] | [[Category: vitamin d3 analogue]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:35 2008'' |
Revision as of 11:19, 21 February 2008
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A Structural Basis for the Unique Binding Features of the Human Vitamin D-binding Protein
Contents |
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 and 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
Page seeded by OCA on Thu Feb 21 13:19:35 2008
