Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon.

@article{Stetefeld2003CollagenSA,
  title={Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon.},
  author={J{\"o}rg Stetefeld and Sabine Frank and Margrit Jenny and Therese Schulthess and Richard A. Kammerer and Sergei P. Boudko and Ruth Landwehr and Kenji Okuyama and J{\"u}rgen Engel},
  journal={Structure},
  year={2003},
  volume={11 3},
  pages={339-46}
}
In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 A resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5 degrees between the symmetry… CONTINUE READING

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