2kc0: Difference between revisions
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==Solution structure of the factor H binding protein== | |||
<StructureSection load='2kc0' size='340' side='right'caption='[[2kc0]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2kc0]] 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=2KC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KC0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kc0 OCA], [https://pdbe.org/2kc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kc0 RCSB], [https://www.ebi.ac.uk/pdbsum/2kc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kc0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6QCC2_NEIME Q6QCC2_NEIME] | |||
== 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/kc/2kc0_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2kc0 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Factor H-binding protein is a 27-kDa lipoprotein of Neisseria meningitidis discovered while screening the bacterial genome for vaccine candidates. In addition to being an important component of a vaccine against meningococcus in late stage of development, the protein is essential for pathogenesis because it allows the bacterium to survive and grow in human blood by binding the human complement factor H. We recently reported the solution structure of the C-terminal domain of factor H-binding protein, which contains the immunodominant epitopes. In the present study, we report the structure of the full-length molecule, determined by nuclear magnetic resonance spectroscopy. The protein is composed of two independent barrels connected by a short link. Mapping the residues recognized by monoclonal antibodies with bactericidal or factor H binding inhibition properties allowed us to predict the sites involved in the function of the protein. The structure therefore provides the basis for designing improved vaccine molecules. | |||
Solution structure of the factor H-binding protein, a survival factor and protective antigen of Neisseria meningitidis.,Cantini F, Veggi D, Dragonetti S, Savino S, Scarselli M, Romagnoli G, Pizza M, Banci L, Rappuoli R J Biol Chem. 2009 Apr 3;284(14):9022-6. Epub 2009 Feb 4. PMID:19196709<ref>PMID:19196709</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2kc0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Neisseria meningitidis]] | |||
[[Category: Banci L]] | |||
[[Category: Cantini F]] | |||
[[Category: Dragonetti S]] | |||
[[Category: Pizza M]] | |||
[[Category: Rappuoli R]] | |||
[[Category: Romagnoli G]] | |||
[[Category: Savino S]] | |||
[[Category: Scarselli M]] | |||
[[Category: Veggi D]] | |||
Latest revision as of 22:11, 29 May 2024
Solution structure of the factor H binding proteinSolution structure of the factor H binding protein
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFactor H-binding protein is a 27-kDa lipoprotein of Neisseria meningitidis discovered while screening the bacterial genome for vaccine candidates. In addition to being an important component of a vaccine against meningococcus in late stage of development, the protein is essential for pathogenesis because it allows the bacterium to survive and grow in human blood by binding the human complement factor H. We recently reported the solution structure of the C-terminal domain of factor H-binding protein, which contains the immunodominant epitopes. In the present study, we report the structure of the full-length molecule, determined by nuclear magnetic resonance spectroscopy. The protein is composed of two independent barrels connected by a short link. Mapping the residues recognized by monoclonal antibodies with bactericidal or factor H binding inhibition properties allowed us to predict the sites involved in the function of the protein. The structure therefore provides the basis for designing improved vaccine molecules. Solution structure of the factor H-binding protein, a survival factor and protective antigen of Neisseria meningitidis.,Cantini F, Veggi D, Dragonetti S, Savino S, Scarselli M, Romagnoli G, Pizza M, Banci L, Rappuoli R J Biol Chem. 2009 Apr 3;284(14):9022-6. Epub 2009 Feb 4. PMID:19196709[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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