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1ma9

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(New page: 200px<br /> <applet load="1ma9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ma9, resolution 2.40&Aring;" /> '''Crystal structure o...)
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Revision as of 16:03, 12 November 2007

Image:1ma9.gif

1ma9, resolution 2.40Å

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

Contents

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.

Disease

Known disease associated with this structure: Graves disease, susceptibility to, 3 OMIM:[139200]

About this Structure

1MA9 is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus with MG and ATP as ligands. 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

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