1ma9
| |||||||
| , 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
Page seeded by OCA on Thu Mar 20 12:40:58 2008