1j78

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(New page: 200px<br /> <applet load="1j78" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j78, resolution 2.31&Aring;" /> '''Crystallographic an...)
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[[Image:1j78.gif|left|200px]]<br />
 
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<applet load="1j78" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1j78, resolution 2.31&Aring;" />
 
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'''Crystallographic analysis of the human vitamin D binding protein'''<br />
 
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==Overview==
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==Crystallographic analysis of the human vitamin D binding protein==
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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.
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<StructureSection load='1j78' size='340' side='right'caption='[[1j78]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1j78]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The November 2012 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Vitamin D Receptor'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2012_11 10.2210/rcsb_pdb/mom_2012_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J78 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.31&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j78 OCA], [https://pdbe.org/1j78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j78 RCSB], [https://www.ebi.ac.uk/pdbsum/1j78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j78 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VTDB_HUMAN VTDB_HUMAN] Multifunctional protein found in plasma, ascitic fluid, cerebrospinal fluid, and urine and on the surface of many cell types. In plasma, it carries the vitamin D sterols and prevents polymerization of actin by binding its monomers. DBP associates with membrane-bound immunoglobulin on the surface of B-lymphocytes and with IgG Fc receptor on the membranes of T-lymphocytes.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j7/1j78_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1j78 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==Disease==
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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<ref>PMID:11799400</ref>
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Known disease associated with this structure: Graves disease, susceptibility to, 3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=139200 139200]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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].
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</div>
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<div class="pdbe-citations 1j78" style="background-color:#fffaf0;"></div>
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==Reference==
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== References ==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11799400 11799400]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Baelen, H.Van.]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Bouillon, R.]]
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[[Category: Vitamin D Receptor]]
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[[Category: Maeyer, M.De.]]
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[[Category: Bouillon R]]
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[[Category: Rabijns, A.]]
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[[Category: De Maeyer M]]
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[[Category: Ranter, C.De.]]
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[[Category: De Ranter C]]
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[[Category: Verboven, C.]]
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[[Category: Rabijns A]]
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[[Category: OLA]]
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[[Category: Van Baelen H]]
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[[Category: VDY]]
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[[Category: Verboven C]]
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[[Category: actin binding]]
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[[Category: fatty acid binding]]
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[[Category: gc-globulin]]
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[[Category: group-specific component]]
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[[Category: plasma protein]]
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[[Category: vitamin d binding]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:37:40 2007''
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Current revision

Crystallographic analysis of the human vitamin D binding protein

PDB ID 1j78

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