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Article

Structural and functional analysis of the tandem β-zipper interaction of a Streptococcal protein with human fibronectin.

The Journal of biological chemistry - 4 Nov 2011

Norris Nicole C, Bingham Richard J, Harris Gemma, Speakman Adrian, Jones Richard P O, Leech Andrew, Turkenburg Johan P, Potts Jennifer R

Abstract excerpt

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...

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Identifiers

PMID: 21840989
DOI: 10.1074/jbc.M111.276592
PMCID: PMC3207447

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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