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Title: Actin-DBP: the perfect structural fit?
Authors: Verboven, Christel ×
Bogaerts, Ilse
Waelkens, Etienne
Rabijns, Anja
Van Baelen, Hugo
Bouillon, Roger
De Ranter, Camiel #
Issue Date: Jan-2003
Publisher: Published for the International Union of Crystallography by Munksgaard
Series Title: Acta Crystallographica. Section D, Biological Crystallography vol:59 issue:Pt 2 pages:263-73
Abstract: 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.
URI: 
ISSN: 0907-4449
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Phosphoproteomics (-)
Biocrystallography
Clinical and Experimental Endocrinology
Laboratory of Protein Phosphorylation and Proteomics
× corresponding author
# (joint) last author

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