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Originally published In Press as doi:10.1074/mcp.M200064-MCP200 on October 11, 2002.
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Molecular & Cellular Proteomics 1:868-875, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Structural Models of Osteogenesis Imperfecta-associated Variants in the COL1A1 Gene*

Sean D. Mooney and Teri E. Klein{ddagger}

From the Department of Genetics, School of Medicine, Stanford University, Stanford, California 94305

Osteogenesis imperfecta (OI) is a genetic disease in which the most common mutations result in substitutions for glycine residues in the triple helical domain of the chains of type I collagen. Currently there is no way to use sequence information to predict the clinical OI phenotype. However, structural models coupled with biophysical and machine learning methods may be able to predict sequences that, when mutated, would be associated with more severe forms of OI. To build appropriate structural models, we have applied a high throughput molecular dynamic approach. Homotrimeric peptides covering 57 positions in which mutations are associated with OI were simulated both with and without mutations. Our models revealed structural differences that occur with different substituting amino acids. When mutations were introduced, we observed a decrease in helix stability, as caused by fewer main chain backbone hydrogen bonds, and an increase in main chain root mean square deviation and specifically bound water molecules.

{ddagger} To whom correspondence should be addressed: Dept. of Genetics, Stanford University, 251 Campus Dr., MSOB x-215, Stanford, CA 94305-5479. Tel.: 650-736-0156; Fax: 650-725-7944; E-mail: teri.klein{at}stanford.edu


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