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Sequence dependent conformational variations of collagen triple-helical structure

Nature Structural Biology volume 6, pages 454–457 (1999)Cite this article

Abstract

The 2 Å crystal structure reported here of the collagen-like model peptide, T3-785, provides the first visualization of how the sequence of collagen defines distinctive local conformational variations in triple-helical structure.

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Figure 1: a, A partial sequence from human type III collagen35 and the sequence of the T3-785 peptide.
Figure 2: Cα traces of the T3-785 model (thick lines) superimposed with those of idealized models (thin lines).

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Acknowledgements

The T3-785 peptide was synthesized by J. Lin. We are grateful to S. C. Jain, J. Liu, G. N. Parkinson, and L. Vitagliano for their many helpful discussions. This work was supported by grants from NIH.

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Author notes

  1. Jordi Bella

    Present address: Department of Biological Sciences, Purdue University, West Lafayette, Indiana, 47907, USA

Authors and Affiliations

  1. Department of Chemistry, Rutgers University, 610 Taylor Rd, Piscataway, 08854-8087 , New Jersey, USA

    Rachel Z. Kramer, Jordi Bella, Patricia Mayville & Helen M. Berman

  2. Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, 08854, New Jersey, USA

    Barbara Brodsky

  3. Waksman Institute, Piscataway, 08855, New Jersey, USA

    Helen M. Berman

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  1. Rachel Z. Kramer
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  5. Helen M. Berman
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Correspondence to Helen M. Berman.

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Kramer, R., Bella, J., Mayville, P. et al. Sequence dependent conformational variations of collagen triple-helical structure. Nat Struct Mol Biol 6, 454–457 (1999). https://doi.org/10.1038/8259

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