1MA9

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

Summary for 1MA9

• Entry DOI: 10.2210/pdb1ma9/pdb
• Related: 1ATN 1J78 1J7E
• Descriptor: Vitamin D-binding protein, Actin, Alpha Skeletal Muscle, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: protein-protein complex, complex formed in plasma, actin scavenger system, transport protein-contractile protein complex, transport protein/contractile protein
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P02774; Cytoplasm, cytoskeleton: P68135
• Total number of polymer chains: 2
• Total formula weight: 93698.43

Authors

Verboven, C.,Bogaerts, I.,Waelkens, E.,Rabijns, A.,Van Baelen, H.,Bouillon, R.,De Ranter, C. (deposition date: 2002-08-02, release date: 2003-02-04, Last modification date: 2011-07-13)

Primary citation

Verboven, C.,Bogaerts, I.,Waelkens, E.,Rabijns, A.,Van Baelen, H.,Bouillon, R.,De Ranter, C.
Actin-DBP: the perfect structural fit?
Acta Crystallogr.,Sect.D, 59:263-273, 2003

PubMed 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.

PubMed: 12554937
DOI: 10.1107/S0907444902021455

Experimental method

X-RAY DIFFRACTION (2.4 Å)