1j78: Difference between revisions

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New page: left|200px<br /> <applet load="1j78" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j78, resolution 2.31Å" /> '''Crystallographic an...
 
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[[Image:1j78.gif|left|200px]]<br />
[[Image:1j78.gif|left|200px]]<br /><applet load="1j78" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1j78" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1j78, resolution 2.31&Aring;" />
caption="1j78, resolution 2.31&Aring;" />
'''Crystallographic analysis of the human vitamin D binding protein'''<br />
'''Crystallographic analysis of the human vitamin D binding protein'''<br />


==Overview==
==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.
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==
1J78 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 OLA and VDY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J78 OCA].  
1J78 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=OLA:'>OLA</scene> and <scene name='pdbligand=VDY:'>VDY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J78 OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Baelen, H.Van.]]
[[Category: Baelen, H Van.]]
[[Category: Bouillon, R.]]
[[Category: Bouillon, R.]]
[[Category: Maeyer, M.De.]]
[[Category: Maeyer, M De.]]
[[Category: Rabijns, A.]]
[[Category: Rabijns, A.]]
[[Category: Ranter, C.De.]]
[[Category: Ranter, C De.]]
[[Category: Verboven, C.]]
[[Category: Verboven, C.]]
[[Category: OLA]]
[[Category: OLA]]
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[[Category: vitamin d binding]]
[[Category: vitamin d binding]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:37:40 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:26 2008''

Revision as of 14:19, 21 February 2008

File:1j78.gif


1j78, resolution 2.31Å

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Crystallographic analysis of the human vitamin D binding protein

OverviewOverview

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.

DiseaseDisease

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

About this StructureAbout this Structure

1J78 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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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