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1ma9

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[[Image:1ma9.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin==
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|PDB= 1ma9 |SIZE=350|CAPTION= <scene name='initialview01'>1ma9</scene>, resolution 2.40&Aring;
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<StructureSection load='1ma9' size='340' side='right'caption='[[1ma9]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
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<table><tr><td colspan='2'>[[1ma9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MA9 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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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=1ma9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ma9 OCA], [https://pdbe.org/1ma9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ma9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ma9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ma9 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/ma/1ma9_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=1ma9 ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin'''
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==See Also==
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*[[Actin 3D structures|Actin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The multifunctional vitamin D binding protein (DBP) is an actin-sequestering protein present in blood. The crystal structure of the actin-DBP complex was determined at 2.4 A resolution. DBP binds to actin subdomains 1 and 3 and occludes the cleft at the interface between these subdomains. Most remarkably, DBP demonstrates an unusually large actin-binding interface, far exceeding the binding-interface areas reported for other actin-binding proteins such as profilin, DNase I and gelsolin. The fast-growing side of actin monomers is blocked completely through a perfect structural fit with DBP, demonstrating how DBP effectively interferes with actin-filament formation. It establishes DBP as the hitherto best actin-sequestering protein and highlights its key role in suppressing and preventing extracellular actin polymerization.
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==Disease==
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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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1MA9 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MA9 OCA].
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==Reference==
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Actin-DBP: the perfect structural fit?, Verboven C, Bogaerts I, Waelkens E, Rabijns A, Van Baelen H, Bouillon R, De Ranter C, Acta Crystallogr D Biol Crystallogr. 2003 Feb;59(Pt 2):263-73. Epub 2003, Jan 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12554937 12554937]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Protein complex]]
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[[Category: Bogaerts I]]
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[[Category: Baelen, H Van.]]
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[[Category: Bouillon R]]
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[[Category: Bogaerts, I.]]
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[[Category: De Ranter C]]
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[[Category: Bouillon, R.]]
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[[Category: Rabijns A]]
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[[Category: Rabijns, A.]]
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[[Category: Van Baelen H]]
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[[Category: Ranter, C De.]]
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[[Category: Verboven C]]
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[[Category: Verboven, C.]]
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[[Category: Waelkens E]]
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[[Category: Waelkens, E.]]
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[[Category: ATP]]
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[[Category: MG]]
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[[Category: actin scavenger system]]
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[[Category: complex formed in plasma]]
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[[Category: protein-protein complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:44:10 2008''
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Current revision

Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin

PDB ID 1ma9

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