Article
Substitutions for arginine at position 780 in triple helical domain of the α1(I) chain alter folding of the type I procollagen molecule and cause osteogenesis imperfecta.
PloS one - 1 Jan 2018
Makareeva Elena, Sun Guoli, Mirigian Lynn S, Mertz Edward L, Vera Juan C, Espinoza Nydea A, Yang Kathleen, Chen Diana, Klein Teri E, Byers Peter H, Leikin Sergey
Abstract excerpt
OI is a clinically and genetically heterogeneous disorder characterized by bone fragility. More than 90% of patients are heterozygous for mutations in type I collagen genes, COL1A1 and COL1A2, and a common mutation is substitution for an obligatory glycine in the triple helical Gly-X-Y repeats. Few non-glycine substitutions in the triple helical domain have been reported; most result in Y-position substitutions...
Topics
- Arginine
- Circular Dichroism
- Collagen Type I
- Humans
- Mutation
- Osteogenesis Imperfecta
- Procollagen
- Protein Folding