1j78: Difference between revisions
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|PDB= 1j78 |SIZE=350|CAPTION= <scene name='initialview01'>1j78</scene>, resolution 2.31Å | |PDB= 1j78 |SIZE=350|CAPTION= <scene name='initialview01'>1j78</scene>, resolution 2.31Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene> | |LIGAND= <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <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= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1j7e|1J7E]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j78 OCA], [http://www.ebi.ac.uk/pdbsum/1j78 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j78 RCSB]</span> | |||
}} | }} | ||
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==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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Ranter, C De.]] | [[Category: Ranter, C De.]] | ||
[[Category: Verboven, C.]] | [[Category: Verboven, C.]] | ||
[[Category: actin binding]] | [[Category: actin binding]] | ||
[[Category: fatty acid binding]] | [[Category: fatty acid binding]] | ||
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[[Category: vitamin d binding]] | [[Category: vitamin d binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:29:29 2008'' | ||
