Structural highlights
Function
Q7BG36_ECOLX
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Afa/Dr family of adhesins are produced by pathogenic Escherichia coli strains that are especially prevalent in chronic diarrhoeal and recurrent urinary tract infections. Most notably, they are found in up to 50% of cystitis cases in children and 30% of pyelonephritis in pregnant women. Afa/Dr adhesins are capped surface fibrils that mediate recognition of the host and subsequent bacterial internalization. Using the newly solved three-dimensional structure of the minimal invasive complex (AfaDE) combined with biochemical and cellular assays, we reveal the architecture of the fibrillar cap and identify a novel mode of synergistic integrin recognition.
The solution structure of the invasive tip complex from Afa/Dr fibrils.,Cota E, Jones C, Simpson P, Altroff H, Anderson KL, du Merle L, Guignot J, Servin A, Le Bouguenec C, Mardon H, Matthews S Mol Microbiol. 2006 Oct;62(2):356-66. Epub 2006 Sep 8. PMID:16965519[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cota E, Jones C, Simpson P, Altroff H, Anderson KL, du Merle L, Guignot J, Servin A, Le Bouguenec C, Mardon H, Matthews S. The solution structure of the invasive tip complex from Afa/Dr fibrils. Mol Microbiol. 2006 Oct;62(2):356-66. Epub 2006 Sep 8. PMID:16965519 doi:10.1111/j.1365-2958.2006.05375.x