Solution structure of the N-terminal F1 module pair from human fibronectin

Jennifer R. Potts, Jeremy R. Bright, David Bolton, Andrew R. Pickford, Iain D. Campbell*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Multiple sites within the N-terminal domain (1-5F1) of fibronectin have been implicated previously in fibronectin matrix assembly, heparin binding, and binding to cell surface proteins of pathogenic bacteria. The solution structure of 1F12F1, the N-terminal F1 module pair from human fibronectin, has been determined using NMR spectroscopy. Both modules in the pair conform to the F1 consensus fold. In 4F15F1, the only other F1 module pair structure available, there is a well-defined intermodule interface; in 1F12F1, however, there is no detectable interface between the modules. Comparison of the backbone 15N-{1H} NOE values for both module pairs confirms that the longer intermodule sequence in 1F12F1 is flexible and that the stabilization of the 4F1 C-D loop observed in 4F15F1, as a result of the intermodule interface, is not observed in 1F12F1.

Original languageEnglish
Pages (from-to)8304-8312
Number of pages9
Issue number26
Publication statusPublished - 29 Jun 1999


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