Abstract
The solution structure of the oligomerization domain of cartilage matrix protein (also known as matrilin-1) has been determined by heteronuclear NMR spectroscopy. The domain folds into a parallel, disulfide-linked, three-stranded, α-helical coiled coil, spanning five heptad repeats in the amino acid sequence. The sequence of the first two heptad repeats shows some deviations from the consensus of hydrophobic and hydrophilic residue preferences. While the corresponding region of the coiled coil has a higher intrinsic flexibility, backbone α-helix and superhelix parameters are consistent with a regular coiled coil structure.
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Acknowledgements
We thank M.J.J. Blommers, W. Jahnke, and W. Stark (Physics, Novartis AG) for encouragement, and for allowing us use of their NMR equipment during all stages of this project; J.L. Markley and T. Schirmer for their comments on the manuscript. This work was supported by grants from EU program Biotechnology II to J.E., and from the Swiss NF to J.E. and A.T.A.
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Dames, S., Kammerer, R., Wiltscheck, R. et al. NMR structure of a parallel homotrimeric coiled coil. Nat Struct Mol Biol 5, 687–691 (1998). https://doi.org/10.1038/90444
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DOI: https://doi.org/10.1038/90444
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