2fvn

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|RELATEDENTRY=[[1rxl|1RXL]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fvn OCA], [http://www.ebi.ac.uk/pdbsum/2fvn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fvn RCSB]</span>
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[[Category: integrin-binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:57:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:08:18 2008''

Revision as of 00:08, 31 March 2008

Image:2fvn.jpg


PDB ID 2fvn

Drag the structure with the mouse to rotate
Related: 1RXL


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins


Overview

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.

About this Structure

2FVN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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