5t5f - Revision history

OCA at 15:36, 6 March 2024

2024-03-06T15:36:48Z

←Older revision		Revision as of 15:36, 6 March 2024
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	<StructureSection load='5t5f' size='340' side='right'caption='[[5t5f]], [[Resolution\|resolution]] 2.98Å' scene=''>		<StructureSection load='5t5f' size='340' side='right'caption='[[5t5f]], [[Resolution\|resolution]] 2.98Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<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>	+	<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>
-	</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>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.98Å</td></tr>
-	<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>	+	<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>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[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>
-	~~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~~.	+
-		+
-	~~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>	+
-		+
-	~~From MEDLINE®~~/~~PubMed®, a database of the U.S. National Library of Medicine.~~<br>	+
-	</~~div~~>	+
-	<~~div class="pdbe-citations 5t5f" style="background-color~~:~~#fffaf0;"~~></~~div~~>	+

	==See Also==		==See Also==
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	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	~~[[Category: Malito, E]]~~	+	[[Category: Neisseria meningitidis]]
-	~~[[Category: Cooperativity]]~~	+	[[Category: Malito E]]
-	~~[[Category: Epitope mapping]]~~	+
-	~~[[Category: Fhbp]]~~	+
-	~~[[Category: Jar5]]~~	+
-	~~[[Category: Monoclonal antibody]]~~	+
-	[[Category: Neisseria ~~meningitidi~~]]	+
-	[[Category: ~~Protein binding~~]]	+

OCA at 11:22, 16 September 2020

2020-09-16T11:22:24Z

←Older revision		Revision as of 11:22, 16 September 2020
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	==Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5==		==Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5==
-	<StructureSection load='5t5f' size='340' side='right' caption='[[5t5f]], [[Resolution\|resolution]] 2.98Å' scene=''>	+	<StructureSection load='5t5f' size='340' side='right'caption='[[5t5f]], [[Resolution\|resolution]] 2.98Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5t5f]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] 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://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5T5F FirstGlance]. <br>	+	<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>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/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>	+	</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>
		+	<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>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	</div>		</div>
	<div class="pdbe-citations 5t5f" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5t5f" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Monoclonal Antibodies 3D structures\|Monoclonal Antibodies 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Malito, E]]		[[Category: Malito, E]]

OCA at 19:58, 9 December 2016

2016-12-09T19:58:41Z

←Older revision		Revision as of 19:58, 9 December 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5t5f is ~~ON HOLD until Paper~~ Publication	+	==Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5==
		+	<StructureSection load='5t5f' size='340' side='right' caption='[[5t5f]], [[Resolution\|resolution]] 2.98Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5t5f]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T5F FirstGlance]. <br>
		+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	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.

-	~~Authors~~: Malito, E.	+	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>

-	~~Description~~: ~~Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5t5f" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Mus musculus]]
	[[Category: Malito, E]]		[[Category: Malito, E]]
		+	[[Category: Cooperativity]]
		+	[[Category: Epitope mapping]]
		+	[[Category: Fhbp]]
		+	[[Category: Jar5]]
		+	[[Category: Monoclonal antibody]]
		+	[[Category: Neisseria meningitidi]]
		+	[[Category: Protein binding]]

OCA: Protected "5t5f" [edit=sysop:move=sysop]

2016-09-09T15:44:09Z

Protected "5t5f" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:44, 9 September 2016

OCA: New page: '''Unreleased structure''' The entry 5t5f is ON HOLD until Paper Publication Authors: Malito, E. Description: Neisseria meningitidis factor H binding protein in complex with monoclonal...

2016-09-09T15:44:07Z

New page: '''Unreleased structure''' The entry 5t5f is ON HOLD until Paper Publication Authors: Malito, E. Description: Neisseria meningitidis factor H binding protein in complex with monoclonal...

New page

'''Unreleased structure'''

The entry 5t5f is ON HOLD until Paper Publication

Authors: Malito, E.

Description: Neisseria meningitidis factor H binding protein in complex with monoclonal antibody JAR5
[[Category: Unreleased Structures]]
[[Category: Malito, E]]