1ys5

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[[Image:1ys5.gif|left|200px]]
 
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==Solution structure of the antigenic domain of GNA1870 of Neisseria meningitidis==
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The line below this paragraph, containing "STRUCTURE_1ys5", creates the "Structure Box" on the page.
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<StructureSection load='1ys5' size='340' side='right'caption='[[1ys5]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ys5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YS5 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ys5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ys5 OCA], [https://pdbe.org/1ys5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ys5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ys5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ys5 ProSAT]</span></td></tr>
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{{STRUCTURE_1ys5| PDB=1ys5 | SCENE= }}
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</table>
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== Function ==
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'''Solution structure of the antigenic domain of GNA1870 of Neisseria meningitidis'''
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[https://www.uniprot.org/uniprot/FHBP_NEIMB FHBP_NEIMB] A bacterial surface lipoprotein that binds host (human) complement factor H (fH, gene CFH), binding contributes to the avoidance of complement-mediated lysis by N.meningitidis. Binding of fH to the bacteria surface is independent of bacterial sialic acid moieties (PubMed:16751403). fH binding affinity is high enough that it may sequester plasma fH, depleting its circulating levels and de-regulating complement in the host (Probable). This protein induces high levels of bactericidal antibodies in mice (PubMed:12642606, PubMed:15039331, PubMed:15664958, PubMed:21753121, PubMed:23133374).<ref>PMID:12642606</ref> <ref>PMID:15039331</ref> <ref>PMID:15664958</ref> <ref>PMID:16751403</ref> <ref>PMID:21753121</ref> <ref>PMID:23133374</ref> <ref>PMID:19225461</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ys/1ys5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ys5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
GNA1870, a 28-kDa surface-exposed lipoprotein of Neisseria meningitidis recently discovered by reverse vaccinology, is one of the most potent antigens of Meningococcus and a promising candidate for a universal vaccine against a devastating disease. Previous studies of epitope mapping and genetic characterization identified residues critical for bactericidal response within the C-terminal domain of the molecule. To elucidate the conformation of protective epitopes, we used NMR spectroscopy to obtain the solution structure of the immunodominant 18-kDa C-terminal portion of GNA1870. The structure consists of an eight-stranded antiparallel beta-barrel overlaid by a short alpha-helix with an unstructured N-terminal end. Residues previously shown to be important for antibody recognition were mapped on loops facing the same ridge of the molecule. The sequence similarity of GNA1870 with members of the bacterial transferrin receptor family allows one to predict the folding of this class of well known bacterial antigens, providing the basis for the rational engineering of high affinity B cell epitopes.
GNA1870, a 28-kDa surface-exposed lipoprotein of Neisseria meningitidis recently discovered by reverse vaccinology, is one of the most potent antigens of Meningococcus and a promising candidate for a universal vaccine against a devastating disease. Previous studies of epitope mapping and genetic characterization identified residues critical for bactericidal response within the C-terminal domain of the molecule. To elucidate the conformation of protective epitopes, we used NMR spectroscopy to obtain the solution structure of the immunodominant 18-kDa C-terminal portion of GNA1870. The structure consists of an eight-stranded antiparallel beta-barrel overlaid by a short alpha-helix with an unstructured N-terminal end. Residues previously shown to be important for antibody recognition were mapped on loops facing the same ridge of the molecule. The sequence similarity of GNA1870 with members of the bacterial transferrin receptor family allows one to predict the folding of this class of well known bacterial antigens, providing the basis for the rational engineering of high affinity B cell epitopes.
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==About this Structure==
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Solution structure of the immunodominant domain of protective antigen GNA1870 of Neisseria meningitidis.,Cantini F, Savino S, Scarselli M, Masignani V, Pizza M, Romagnoli G, Swennen E, Veggi D, Banci L, Rappuoli R J Biol Chem. 2006 Mar 17;281(11):7220-7. Epub 2005 Dec 31. PMID:16407174<ref>PMID:16407174</ref>
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1YS5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YS5 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Solution structure of the immunodominant domain of protective antigen GNA1870 of Neisseria meningitidis., Cantini F, Savino S, Scarselli M, Masignani V, Pizza M, Romagnoli G, Swennen E, Veggi D, Banci L, Rappuoli R, J Biol Chem. 2006 Mar 17;281(11):7220-7. Epub 2005 Dec 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16407174 16407174]
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</div>
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<div class="pdbe-citations 1ys5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Neisseria meningitidis]]
[[Category: Neisseria meningitidis]]
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[[Category: Single protein]]
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[[Category: Banci L]]
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[[Category: Banci, L.]]
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[[Category: Cantini F]]
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[[Category: Cantini, F.]]
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[[Category: Masignani V]]
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[[Category: Masignani, V.]]
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[[Category: Pizza M]]
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[[Category: Pizza, M.]]
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[[Category: Rappuoli R]]
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[[Category: Rappuoli, R.]]
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[[Category: Romagnoli G]]
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[[Category: Romagnoli, G.]]
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[[Category: Savino S]]
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[[Category: Savino, S.]]
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[[Category: Scarselli M]]
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[[Category: Scarselli, M.]]
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[[Category: Swennen E]]
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[[Category: Swennen, E.]]
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[[Category: Veggi D]]
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[[Category: Veggi, D.]]
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[[Category: Beta-barrel structure]]
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[[Category: Neisseria meningitidi]]
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[[Category: Vaccine candidate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:42:54 2008''
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Current revision

Solution structure of the antigenic domain of GNA1870 of Neisseria meningitidis

PDB ID 1ys5

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