1ma9: Difference between revisions

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-[[Image:1ma9.jpg|left|200px]]
+{{Seed}}
+[[Image:1ma9.png|left|200px]]
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 {{STRUCTURE_1ma9|  PDB=1ma9  |  SCENE=  }}
-'''Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin'''
+===Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_12554937}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12554937 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12554937}}
 ==About this Structure==
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 [[Category: Complex formed in plasma]]
 [[Category: Protein-protein complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:49:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 23:32:47 2008''