2fvn
From Proteopedia
(New page: 200px<br /><applet load="2fvn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fvn" /> '''The fibrillar tip complex of the Afa/Dr adhe...) |
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| - | [[Image:2fvn.jpg|left|200px]]<br /><applet load="2fvn" size=" | + | [[Image:2fvn.jpg|left|200px]]<br /><applet load="2fvn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fvn" /> | caption="2fvn" /> | ||
'''The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins'''<br /> | '''The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Afa/Dr family of adhesins are produced by pathogenic Escherichia coli | + | 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== | ==About this Structure== | ||
| - | 2FVN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 2FVN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FVN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Anderson, K | + | [[Category: Anderson, K L.]] |
[[Category: Cota, E.]] | [[Category: Cota, E.]] | ||
| - | [[Category: Matthews, S | + | [[Category: Matthews, S J.]] |
[[Category: Simpson, P.]] | [[Category: Simpson, P.]] | ||
[[Category: afad]] | [[Category: afad]] | ||
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[[Category: integrin-binding]] | [[Category: integrin-binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:33 2008'' |
Revision as of 15:25, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 17:25:33 2008
Categories: Escherichia coli | Single protein | Anderson, K L. | Cota, E. | Matthews, S J. | Simpson, P. | Afad | Afae | Afimbrial | Ceacam | Daec | Daf | Fibrillar | Integrin-binding
