Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding.

@article{Graille2010ZincIS,
  title={Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding.},
  author={M. Graille and M. Pagano and T. Rose and Mich{\`e}le Reboud Ravaux and H. van Tilbeurgh},
  journal={Structure},
  year={2010},
  volume={18 6},
  pages={
          710-8
        }
}
  • M. Graille, M. Pagano, +2 authors H. van Tilbeurgh
  • Published 2010
  • Biology, Medicine
  • Structure
  • Fibronectin is a modular extracellular matrix protein involved in cell adhesion, cell motility, wound healing, and maintenance of cell morphology. [...] Key Result GBD forms a very compact zinc-mediated homodimer, in stark contrast with previous structures of fibronectin fragments. Most remarkably, 8F(I) no longer adopts the canonical F(I) fold but is composed of two long strands that associate with 7F(I) and 9F(I) into a large beta-sheet superdomain.Expand Abstract

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