5t5f

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Current revision (15:36, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5t5f' size='340' side='right'caption='[[5t5f]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
<StructureSection load='5t5f' size='340' side='right'caption='[[5t5f]], [[Resolution|resolution]] 2.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5t5f]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T5F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5T5F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5t5f]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T5F FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fhbp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 "Diplokokkus intracellularis meningitidis" (sic) Weichselbaum 1887])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.98&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5t5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5f OCA], [http://pdbe.org/5t5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t5f RCSB], [http://www.ebi.ac.uk/pdbsum/5t5f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5f ProSAT]</span></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=5t5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5f OCA], [https://pdbe.org/5t5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t5f RCSB], [https://www.ebi.ac.uk/pdbsum/5t5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5f ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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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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Factor H binding protein (fHbp) is an important antigen of Neisseria meningitidis that is able to elicit a robust protective immune response in humans. Previous studies on the interactions of fHbp with antibodies revealed that some anti-fHbp monoclonal antibodies that are unable to trigger complement-mediated bacterial killing in vitro , are highly cooperative and become bactericidal if used in combination. Several factors have been shown to influence such cooperativity, including IgG subclass and antigen density. To investigate the structural basis of the anti-fHbp antibody synergy, we determined the crystal structure of the complex between fHbp and the Fab fragment of JAR5, a specific anti-fHbp murine monoclonal antibody known to be highly cooperative with other monoclonal antibodies. We show that JAR5 is highly synergic with mAb 12C1, whose structure in complex with fHbp has been previously solved. Structural analyses of the epitopes recognized by JAR5 and 12C1, and computational modelling of full-length IgG mAbs of JAR5 and 12C1 bound to the same fHbp molecule provide insights on the spatial orientation of Fc regions and on the possible implications for the susceptibility of meningococci to complement-mediated killing.
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Neisseria meningitidis fac---tor H bin---ding protein bound to monoclonal antibody JAR5: implications for antibody synergy.,Malito E, Lo Surdo P, Veggi D, Santini L, Heather Stefek H, Brunelli B, Luzzi E, Bottomley MJ, Beernink P, Scarselli M Biochem J. 2016 Oct 26. pii: BCJ20160806. PMID:27784765<ref>PMID:27784765</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5t5f" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Malito, E]]
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[[Category: Neisseria meningitidis]]
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[[Category: Cooperativity]]
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[[Category: Malito E]]
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[[Category: Epitope mapping]]
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[[Category: Fhbp]]
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[[Category: Jar5]]
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[[Category: Monoclonal antibody]]
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[[Category: Neisseria meningitidi]]
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[[Category: Protein binding]]
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Current revision

Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5

PDB ID 5t5f

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