1o9a: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1o9a.png|left|200px]]
-<!--
+==Solution structure of the complex of 1F12F1 from fibronectin with B3 from FnBB from S. dysgalactiae==
-The line below this paragraph, containing "STRUCTURE_1o9a", creates the "Structure Box" on the page.
+<StructureSection load='1o9a' size='340' side='right'caption='[[1o9a]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1o9a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Streptococcus_dysgalactiae Streptococcus dysgalactiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O9A FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o9a OCA], [https://pdbe.org/1o9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o9a RCSB], [https://www.ebi.ac.uk/pdbsum/1o9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o9a ProSAT]</span></td></tr>
-{{STRUCTURE_1o9a|  PDB=1o9a  |  SCENE=  }}
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN] Defects in FN1 are the cause of glomerulopathy with fibronectin deposits type 2 (GFND2) [MIM:[https://omim.org/entry/601894 601894]; also known as familial glomerular nephritis with fibronectin deposits or fibronectin glomerulopathy. GFND is a genetically heterogeneous autosomal dominant disorder characterized clinically by proteinuria, microscopic hematuria, and hypertension that leads to end-stage renal failure in the second to fifth decade of life.<ref>PMID:18268355</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/FINC_HUMAN FINC_HUMAN] Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref>   Anastellin binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.<ref>PMID:8114919</ref> <ref>PMID:11209058</ref> <ref>PMID:15665290</ref> <ref>PMID:19379667</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o9/1o9a_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o9a ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3 FROM FNBB FROM S. DYSGALACTIAE===
+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<ref>PMID:12736686</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1o9a" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_12736686}}, adds the Publication Abstract to the page
+*[[Fibronectin 3D structures|Fibronectin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 12736686 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12736686}}
+__TOC__
+</StructureSection>
-==About this Structure==
-O9A is a 2 chains 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==
-<ref group="xtra">PMID:12736686</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Briggs, J A.G.]]
+[[Category: Large Structures]]
-[[Category: Campbell, I D.]]
+[[Category: Streptococcus dysgalactiae]]
-[[Category: Gough, T S.]]
+[[Category: Briggs JAG]]
-[[Category: Gurusiddappa, S.]]
+[[Category: Campbell ID]]
-[[Category: Hook, M.]]
+[[Category: Gurusiddappa S]]
-[[Category: Kim, J H.]]
+[[Category: Hook M]]
-[[Category: Pickford, A R.]]
+[[Category: Pickford AR]]
-[[Category: Pilka, E S.]]
+[[Category: Pilka ES]]
-[[Category: Potts, J R.]]
+[[Category: Potts JR]]
-[[Category: Schwarz-Linek, U.]]
+[[Category: Schwarz-Linek U]]
-[[Category: Werner, J M.]]
+[[Category: Werner JM]]
-[[Category: Host-pathogen protein complex,cell adhesion,fibronectin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:34:14 2009''