1ma9: Difference between revisions

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|PDB= 1ma9 |SIZE=350|CAPTION= <scene name='initialview01'>1ma9</scene>, resolution 2.40&Aring;
|PDB= 1ma9 |SIZE=350|CAPTION= <scene name='initialview01'>1ma9</scene>, resolution 2.40&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-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.
==Disease==
Known disease associated with this structure: Graves disease, susceptibility to, 3 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=139200 139200]]


==About this Structure==
==About this Structure==
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[[Category: Verboven, C.]]
[[Category: Verboven, C.]]
[[Category: Waelkens, E.]]
[[Category: Waelkens, E.]]
[[Category: ATP]]
[[Category: MG]]
[[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]]


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