1ma9
From Proteopedia
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'''Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin''' | '''Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin''' | ||
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[[Category: Verboven, C.]] | [[Category: Verboven, C.]] | ||
[[Category: Waelkens, E.]] | [[Category: Waelkens, E.]] | ||
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| - | [[Category: | + | [[Category: Complex formed in plasma]] |
| - | [[Category: | + | [[Category: Protein-protein complex]] |
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Revision as of 21:49, 2 May 2008
Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin
Overview
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.
About this Structure
1MA9 is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 00:49:15 2008
