2fvn: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
[[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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FVN OCA].  
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.L.]]
[[Category: Anderson, K L.]]
[[Category: Cota, E.]]
[[Category: Cota, E.]]
[[Category: Matthews, S.J.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:47:42 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:33 2008''