Collagen Disease Triple helical structure

Many epidemiological, clinical, genetic, and biochemical studies have been conducted since the first widely recognized descriptions of OI in the 18th century. The disease has been shown to be caused by defective synthesis of type I collagen, a triple helical protein made from two a 1(1)- and one a2(I)-chains with fibers that form the structural frame of bone matrix. 

Another important 2-OG dependent oxygenase in mammals is prolyl-4 hydroxylase, which catalyzes the hydroxylation of the proline residue in collagen (Scheme 5). This reaction is essential for the structure of the collagen triple helices (9,34 6). An overproduction of collagen is related to fibrotic diseases such as rheumatic arthritis. Thus collagen prolyl-4 hydroxylase is a target for therapeutics (34,36). 

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