Journal
IUBMB LIFE
Volume 59, Issue 7, Pages 436-440Publisher
WILEY
DOI: 10.1080/15216540701474523
Keywords
hemoproteins; molecular evolution; protein structure; comparative modeling; docking simulation
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We hypothesize that the structure of the heme binding site of paralogous albuminoids alpha- fetoprotein and serum albumin has evolved from the ancestor vitamin D binding protein through the 'phylogenetic intermediate' afamin, the most recently discovered albuminoid. Heme binding to plasma proteins should serve not only as a bu. er for heme homeostasis, avoiding heme binding to lipoproteins with the consequent oxidative stress, but also for heme transfer to the liver, complementing the function of hemopexin.
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