1j7e

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{{Seed}}
 
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[[Image:1j7e.png|left|200px]]
 
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==A Structural Basis for the Unique Binding Features of the Human Vitamin D-binding Protein==
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The line below this paragraph, containing "STRUCTURE_1j7e", creates the "Structure Box" on the page.
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<StructureSection load='1j7e' size='340' side='right'caption='[[1j7e]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1j7e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J7E FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.55&#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=JY:3-(2-{4-[2-(5-HYDROXY-2-METHYLENE-CYCLOHEXYLIDENE)-ETHYLIDENE]-7A-METHYL-OCTAHYDRO-INDEN-1-YL}-PROPYL)-PHENOL'>JY</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene></td></tr>
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{{STRUCTURE_1j7e| PDB=1j7e | SCENE= }}
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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=1j7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j7e OCA], [https://pdbe.org/1j7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j7e RCSB], [https://www.ebi.ac.uk/pdbsum/1j7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j7e 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/j7/1j7e_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1j7e 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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===A Structural Basis for the Unique Binding Features of the Human Vitamin D-binding Protein===
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_11799400}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1j7e" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11799400 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11799400}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1J7E is a 2 chains structure of sequences 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=1J7E OCA].
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==Reference==
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<ref group="xtra">PMID:11799400</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Baelen, H Van.]]
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[[Category: Large Structures]]
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[[Category: Bouillon, R.]]
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[[Category: Bouillon R]]
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[[Category: Maeyer, M De.]]
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[[Category: De Maeyer M]]
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[[Category: Rabijns, A.]]
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[[Category: De Ranter C]]
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[[Category: Ranter, C De.]]
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[[Category: Rabijns A]]
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[[Category: Verboven, C.]]
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[[Category: Van Baelen H]]
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[[Category: Gc-globulin]]
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[[Category: Verboven C]]
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[[Category: Group-specific component]]
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[[Category: Vitamin d binding]]
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[[Category: Vitamin d3 analogue]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:34:41 2009''
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Current revision

A Structural Basis for the Unique Binding Features of the Human Vitamin D-binding Protein

PDB ID 1j7e

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