1ma9: Difference between revisions
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|PDB= 1ma9 |SIZE=350|CAPTION= <scene name='initialview01'>1ma9</scene>, resolution 2.40Å | |PDB= 1ma9 |SIZE=350|CAPTION= <scene name='initialview01'>1ma9</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1j78|1J78]], [[1j7e|1J7E]], [[1atn|1ATN]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ma9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ma9 OCA], [http://www.ebi.ac.uk/pdbsum/1ma9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ma9 RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Verboven, C.]] | [[Category: Verboven, C.]] | ||
[[Category: Waelkens, E.]] | [[Category: Waelkens, E.]] | ||
[[Category: actin scavenger system]] | [[Category: actin scavenger system]] | ||
[[Category: complex formed in plasma]] | [[Category: complex formed in plasma]] | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:13:32 2008'' | ||
Revision as of 22:13, 30 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | , , | ||||||
| Related: | 1J78, 1J7E, 1ATN
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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.
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
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