Disulfide bonding as a determinant of the molecular composition of types I, II and III procollagen.
Procollagen molecules have amino-terminal and carboxy-terminal propeptides at the respective ends of the collagenous triple helix. The carboxy-terminal propeptides enhance and direct the association of pro alpha-chains into procollagen molecules, but the mechanism of this registration function is still obscure. A hypothesis concerning the function of disulfide bonding in the assembly of types I, II and III procollagen is put forward here.
D007535:Isomerases / Q000378:metabolism; D008954:Models, Biological; D011347:Procollagen / Q000378:metabolism; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational
D011347:Procollagen; D007535:Isomerases