Article
The effects of different cysteine for glycine substitutions within alpha 2(I) chains. Evidence of distinct structural domains within the type I collagen triple helix.
The Journal of biological chemistry - 5 Feb 1991
Wenstrup R J, Shrago-Howe A W, Lever L W, Phillips C L, Byers P H, Cohn D H
Abstract excerpt
Affected individuals from two apparently distinct, mild osteogenesis imperfecta families were heterozygous for a G to T transition in the COL1A2 gene that resulted in cysteine for glycine substitutions at position 646 in the alpha 2(I) chain of type I collagen. A child with a moderately severe fo...
Topics
- Amino Acid Sequence
- Base Sequence
- Cells, Cultured
- Child
- Cloning, Molecular
- Cysteine
- Female
- Glycine
- Heterozygote
- Humans
- Molecular Sequence Data
- Mutation
- Osteogenesis Imperfecta
- Procollagen
- Protein Conformation
- Protein Denaturation
- Temperature