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High-resolution structural studies of the factor Xllla crosslinking site and the first type 1 module of fibronectin

Nature Structural Biology volume 2, pages 946–950 (1995)Cite this article

The N-terminal domain of fibronectin undergoes factor XIIIa-catalysed crosslinking to fibrin, bacteria and collagen. The reactive glutamine residue is in an extended, random coil ‘tail’ of about 18 residues that would be accessible for crosslinking.

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Author information

Author notes

  1. Michael J. Williams

    Present address: Department of Vascular Biology, The Scripps Research Institute, 10666 N. Torrey Pines Road, La Jolla, California, 92037, USA

Authors and Affiliations

  1. Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK

    Jennifer R. Potts, Isabelle Phan & Iain D. Campbell

Authors
  1. Jennifer R. Potts
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  2. Isabelle Phan
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  3. Michael J. Williams
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  4. Iain D. Campbell
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Potts, J., Phan, I., Williams, M. et al. High-resolution structural studies of the factor Xllla crosslinking site and the first type 1 module of fibronectin. Nat Struct Mol Biol 2, 946–950 (1995). https://doi.org/10.1038/nsb1195-946

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