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).

Download

Full text not available from this repository.

Description/Abstract

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 β-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
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
Date Deposited: 07 Aug 2008
Last Modified: 27 Mar 2014 18:39
URI: http://eprints.soton.ac.uk/id/eprint/56614

Actions (login required)

View Item View Item