1ma9: Difference between revisions

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|PDB= 1ma9 |SIZE=350|CAPTION= <scene name='initialview01'>1ma9</scene>, resolution 2.40&Aring;
|PDB= 1ma9 |SIZE=350|CAPTION= <scene name='initialview01'>1ma9</scene>, resolution 2.40&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
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[[Category: protein-protein complex]]
[[Category: protein-protein complex]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:40:58 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:44:10 2008''

Revision as of 13:44, 23 March 2008

File:1ma9.jpg


PDB ID 1ma9

Drag the structure with the mouse to rotate
, resolution 2.40Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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.

DiseaseDisease

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

About this StructureAbout this Structure

1MA9 is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

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:12554937

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