Structural insight into binding of Staphylococcus aureus to human fibronectin

Pilka, Ewa S., Werner, Joern M., Schwarz-Linek, Ulrich, Pickford, Andrew R., Meenan, Nicola A.G., Campbell, Iain D. and Potts, Jennifer R. (2006) Structural insight into binding of Staphylococcus aureus to human fibronectin. FEBS Letters, 580, (1), 273-277. (doi:10.1016/j.febslet.2005.12.008).


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Staphylococcus aureus possesses cell-wall attached proteins that bind the human protein fibronectin (Fn). An intermodule interface between the 4F1 and 5F1 modules in the N-terminal domain of Fn is maintained on bacterial peptide binding but there is a small change in the intermodule orientation and alignment of ?-strands that are predicted to bind the peptide. The module pair is elongated, as in the unbound state. Combined with evidence that residues in both 4F1 and 5F1 are directly involved in peptide binding, this observation supports the hypothesis that, when bound to intact Fn, the bacterial protein adopts an unusual, highly extended conformation.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1016/j.febslet.2005.12.008
ISSNs: 0014-5793 (print)
Related URLs:
Keywords: fibronectin, nmr, Staphylococcus aureus
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions : University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 56614
Accepted Date and Publication Date:
9 January 2006Published
10 October 2005Submitted
Date Deposited: 07 Aug 2008
Last Modified: 31 Mar 2016 12:37

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