1o9a: Difference between revisions

Revision as of 23:16, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1o9a.png

Template:STRUCTURE 1o9a

SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3 FROM FNBB FROM S. DYSGALACTIAESOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3 FROM FNBB FROM S. DYSGALACTIAE

Template:ABSTRACT PUBMED 12736686

About this StructureAbout this Structure

1O9A is a Protein complex structure of sequences from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper., Schwarz-Linek U, Werner JM, Pickford AR, Gurusiddappa S, Kim JH, Pilka ES, Briggs JA, Gough TS, Hook M, Campbell ID, Potts JR, Nature. 2003 May 8;423(6936):177-81. PMID:12736686

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OCA

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-[[Image:1o9a.gif|left|200px]]
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 {{STRUCTURE_1o9a|  PDB=1o9a  |  SCENE=  }}
-'''SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3 FROM FNBB FROM S. DYSGALACTIAE'''
+===SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3 FROM FNBB FROM S. DYSGALACTIAE===
-==Overview==
+<!--
-Staphylococcus aureus and Streptococcus pyogenes, two important human pathogens, target host fibronectin (Fn) in their adhesion to and invasion of host cells. Fibronectin-binding proteins (FnBPs), anchored in the bacterial cell wall, have multiple Fn-binding repeats in an unfolded region of the protein. The bacterium-binding site in the amino-terminal domain (1-5F1) of Fn contains five sequential Fn type 1 (F1) modules. Here we show the structure of a streptococcal (S. dysgalactiae) FnBP peptide (B3) in complex with the module pair 1F12F1. This identifies 1F1- and 2F1-binding motifs in B3 that form additional antiparallel beta-strands on sequential F1 modules-the first example of a tandem beta-zipper. Sequence analyses of larger regions of FnBPs from S. pyogenes and S. aureus reveal a repeating pattern of F1-binding motifs that match the pattern of F1 modules in 1-5F1 of Fn. In the process of Fn-mediated invasion of host cells, therefore, the bacterial proteins seem to exploit the modular structure of Fn by forming extended tandem beta-zippers. This work is a vital step forward in explaining the full mechanism of the integrin-dependent FnBP-mediated invasion of host cells.
+The line below this paragraph, {{ABSTRACT_PUBMED_12736686}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12736686 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12736686}}
 ==About this Structure==
-O9A is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9A OCA].
+O9A is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9A OCA].
 ==Reference==
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 [[Category: Werner, J M.]]
 [[Category: Host-pathogen protein complex,cell adhesion,fibronectin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:32:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:16:31 2008''