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A more recent version of this article appeared on November 1, 2002.
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Submitted on September 29, 2002
Revised on October 11, 2002
Accepted on October 11, 2002

Structural models of osteogenesis imperfecta associated variants in the COL1A1 gene

Sean D. Mooney and Teri E. Klein

Genetics, Stanford University, Stanford, California 94305-5479

Corresponding Author: teri.klein{at}stanford.edu

Osteogenesis Imperfecta 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 dynamics 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 RMSD and specifically bound water molecules.


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