1ma9 | pdb_00001ma9

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

spinqualitylabelsall models 1ma9, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ma9 is a 2 chain structure with sequence from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, MG NonStd Res: HIC Related: 1j78, 1j7e, 1atn Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Actin

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