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. Author manuscript; available in PMC: 2020 Jul 27.
Published in final edited form as: Lancet. 2015 Nov 3;387(10028):1657–1671. doi: 10.1016/S0140-6736(15)00728-X

Figure 1: Mutations in specific positions along type I procollagen molecule cause distinct clinical phenotypes.

Figure 1:

Mutations affecting the helical region of the α chains and the C-propeptide domain cause classic osteogenesis imperfecta, including the osteogenesis imperfecta/Ehlers-Danlos syndrome variant, which is caused by substitutions in the N-anchor domain. Molecular defects in the N-propeptide cleavage site cause Ehlers-Danlos syndrome VII A/B and in the C-propeptide cleavage site cause high bone mass osteogenesis imperfecta. Hexagons represent sugar molecules linked to hydroxyl lysine residues. OH-=hydroxyl group linked to proline or lysine residues.