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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
47
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pubmed:dateCreated |
2010-11-15
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pubmed:abstractText |
Fibronectin-binding proteins (FnBPs) of Staphylococcus aureus and Streptococcus pyogenes mediate invasion of human endothelial and epithelial cells in a process likely to aid the persistence and/or dissemination of infection. In addition to binding sites for the N-terminal domain (NTD) of fibronectin (Fn), a number of streptococcal FnBPs also contain an upstream region (UR) that is closely associated with an NTD-binding region; UR binds to the adjacent gelatin-binding domain (GBD) of Fn. Previously, UR was shown to be required for efficient streptococcal invasion of epithelial cells. Here we show, using a Streptococcus zooepidemicus FnBP, that the UR-binding site in GBD resides largely in the (8)F1(9)F1 module pair. We also show that UR inhibits binding of a peptide from the ?1 chain of type I collagen to (8)F1(9)F1 and that UR binding to (8)F1 is likely to occur through anti-parallel ?-zipper formation. Thus, we propose that streptococcal proteins that contain adjacent NTD- and GBD-binding sites form a highly unusual extended tandem ?-zipper that spans the two domains and mediates high affinity binding to Fn through a large intermolecular interface. The proximity of the UR- and NTD-binding sequences in streptococcal FnBPs is consistent with a non-linear arrangement of modules in the tertiary structure of the GBD of Fn.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-10547349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-10627045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-11207605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-11285216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-11292701,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-11323441,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-11349087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-11736995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-12117986,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-12736686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-1386839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-15236673,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-15247227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-15385465,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-15563605,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-15737988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-16083879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-16782385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-17464288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-18713862,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-19251642,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-19366708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-19407246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-20107040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-2521391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-2757186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-3928622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-7833045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-8193122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20843804-8926060
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1083-351X
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pubmed:author |
pubmed-author:AtkinKate EKE,
pubmed-author:BinghamRichard JRJ,
pubmed-author:BrentnallAndrew SAS,
pubmed-author:CampbellIain DID,
pubmed-author:EratMichele CMC,
pubmed-author:HarrisGemmaG,
pubmed-author:MillardChristopher JCJ,
pubmed-author:PottsJennifer RJR,
pubmed-author:Schwarz-LinekUlrichU,
pubmed-author:StauntonDavidD,
pubmed-author:VakonakisIoannisI
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pubmed:issnType |
Electronic
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pubmed:day |
19
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pubmed:volume |
285
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
36977-83
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pubmed:dateRevised |
2011-7-20
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pubmed:meshHeading |
pubmed-meshheading:20843804-Amino Acid Sequence,
pubmed-meshheading:20843804-Binding Sites,
pubmed-meshheading:20843804-Crystallography, X-Ray,
pubmed-meshheading:20843804-Fibronectins,
pubmed-meshheading:20843804-Gelatin,
pubmed-meshheading:20843804-Humans,
pubmed-meshheading:20843804-Magnetic Resonance Spectroscopy,
pubmed-meshheading:20843804-Models, Molecular,
pubmed-meshheading:20843804-Molecular Sequence Data,
pubmed-meshheading:20843804-Protein Binding,
pubmed-meshheading:20843804-Protein Conformation,
pubmed-meshheading:20843804-Protein Structure, Tertiary,
pubmed-meshheading:20843804-Recombinant Proteins,
pubmed-meshheading:20843804-Sequence Homology, Amino Acid,
pubmed-meshheading:20843804-Streptococcus equi
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pubmed:year |
2010
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pubmed:articleTitle |
The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules.
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pubmed:affiliation |
Department of Biology, University of York, Heslington, York, YO10 5DD, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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