1j78
From Proteopedia
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| - | [[Image:1j78.gif|left|200px]] | + | [[Image:1j78.gif|left|200px]] |
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| - | '''Crystallographic analysis of the human vitamin D binding protein''' | + | {{Structure |
| + | |PDB= 1j78 |SIZE=350|CAPTION= <scene name='initialview01'>1j78</scene>, resolution 2.31Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene> and <scene name='pdbligand=VDY:3-{2-[1-(5-HYDROXY-1,5-DIMETHYL-HEXYL)-7A-METHYL-OCTAHYDRO-INDEN-4-YLIDENE]-ETHYLIDENE}-4-METHYLENE-CYCLOHEXANOL'>VDY</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystallographic analysis of the human vitamin D binding protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1J78 is a [ | + | 1J78 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J78 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11799400 11799400] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: vitamin d binding]] | [[Category: vitamin d binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:59:29 2008'' |
Revision as of 09:59, 20 March 2008
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| , resolution 2.31Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystallographic analysis 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
1J78 is a Single protein structure of sequence from Homo sapiens. 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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