Structural and functional analysis of the tandem β-zipper interaction of a streptococcal protein with human fibronectin
Bacterial fibronectin-binding proteins (FnBPs) contain a large intrinsically disordered region (IDR) that mediates adhesion of bacteria to host tissues, and invasion of host cells, through binding to fibronectin (Fn). These FnBP IDRs consist of Fn-binding repeats (FnBRs) that form a highly extended tandem β-zipper interaction on binding to the N-terminal domain of Fn. Several FnBR residues are highly conserved across bacterial species, and here we investigate their contribution to the...[Show more]
|Collections||ANU Research Publications|
|Source:||Journal of Biological Chemistry|
|Access Rights:||Open Access|
|01_Norris_Structural_and_functional_2011.pdf||2.5 MB||Adobe PDF|
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