1ma9
From Proteopedia
(New page: 200px<br /> <applet load="1ma9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ma9, resolution 2.40Å" /> '''Crystal structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ma9. | + | [[Image:1ma9.jpg|left|200px]]<br /><applet load="1ma9" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ma9" size=" | + | |
caption="1ma9, resolution 2.40Å" /> | caption="1ma9, resolution 2.40Å" /> | ||
'''Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin'''<br /> | '''Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1MA9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1MA9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MA9 OCA]. |
==Reference== | ==Reference== | ||
| Line 31: | Line 30: | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:23:17 2008'' |
Revision as of 14:23, 15 February 2008
|
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 Fri Feb 15 16:23:17 2008
