The substitution of arginine for glycine 85 of the alpha 1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen.

Deak, S B; Scholz, P M; Amenta, P S; Constantinou, C D; Levi-Minzi, S A; Gonzalez-Lavin, L; Mackenzie, J W

Deak, S B; Scholz, P M; Amenta, P S; Constantinou, C D; Levi-Minzi, S A; Gonzalez-Lavin, L; Mackenzie, J W.

Affiliation

Deak SB; Department of Surgery, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, New Brunswick 08903.

J Biol Chem ; 266(32): 21827-32, 1991 Nov 15.

Article in En | MEDLINE | ID: mdl-1718984

Subject(s)

Arginine; Glycine; Mutation; Osteogenesis Imperfecta/genetics; Procollagen/genetics; Skin/physiopathology; Amino Acid Sequence; Base Sequence; Blotting, Northern; Cells, Cultured; DNA/genetics; Fibroblasts/physiology; Humans; Macromolecular Substances; Male; Middle Aged; Molecular Sequence Data; Oligodeoxyribonucleotides; Osteogenesis Imperfecta/pathology; Peptide Mapping; Polymerase Chain Reaction/methods; Protein Conformation; Protein Processing, Post-Translational; RNA/genetics; RNA/isolation & purification; Reference Values; Restriction Mapping; Skin/pathology; Skin Physiological Phenomena; Thermodynamics

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Collection: 01-internacional Database: MEDLINE Main subject: Osteogenesis Imperfecta / Arginine / Skin / Procollagen / Glycine / Mutation Limits: Humans / Male / Middle aged Language: En Journal: J Biol Chem Year: 1991 Document type: Article Country of publication: United States

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