1ma9
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The multifunctional vitamin D binding protein (DBP) is an | + | 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== | ==Disease== | ||
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[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Baelen, H | + | [[Category: Baelen, H Van.]] |
[[Category: Bogaerts, I.]] | [[Category: Bogaerts, I.]] | ||
[[Category: Bouillon, R.]] | [[Category: Bouillon, R.]] | ||
[[Category: Rabijns, A.]] | [[Category: Rabijns, A.]] | ||
| - | [[Category: Ranter, C | + | [[Category: Ranter, C De.]] |
[[Category: Verboven, C.]] | [[Category: Verboven, C.]] | ||
[[Category: Waelkens, E.]] | [[Category: Waelkens, E.]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:10 2008'' |
Revision as of 11:53, 21 February 2008
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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 and 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
Page seeded by OCA on Thu Feb 21 13:53:10 2008
