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={Marc Graille and Maurice Pagano and Thierry Rose and Mich{\`e}le Reboud Ravaux and Herman Van Tilbeurgh},
  journal={Structure},
  year={2010},
  volume={18 6},
  pages={710-8}
}
Fibronectin is a modular extracellular matrix protein involved in cell adhesion, cell motility, wound healing, and maintenance of cell morphology. It is composed of multiple repeats of three distinct modules: F(I), F(II), and F(III). Various combinations of these modules create fragments able to interact with different constituents of the extracellular matrix. Here, we present the 2.5-A resolution crystal structure of its 45-kDa gelatin-binding domain (GBD; 6F(I)-1F(II)-2F(II)-7F(I)-8F(I)-9F(I… CONTINUE READING

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Identification and structural analysis of type I collagen sites in complex with fibronectin fragments.

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