4b60 - Revision history

OCA at 11:43, 20 December 2023

2023-12-20T11:43:59Z

← Older revision		Revision as of 11:43, 20 December 2023
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	<StructureSection load='4b60' size='340' side='right'caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>		<StructureSection load='4b60' size='340' side='right'caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4b60]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Staa8 Staa8~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B60 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4b60]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B60 FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~</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]] 1.83Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[4b5z\|4b5z]]~~</~~div~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=4b60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b60 OCA], [https://pdbe.org/4b60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b60 RCSB], [https://www.ebi.ac.uk/pdbsum/4b60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b60 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=4b60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b60 OCA], [https://pdbe.org/4b60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b60 RCSB], [https://www.ebi.ac.uk/pdbsum/4b60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b60 ProSAT]</span></td></tr>
	</table>		</table>
	~~== Disease ==~~
	[[https://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Defects in FGG are a cause of congenital afibrinogenemia (CAFBN) [MIM:[https://omim.org/entry/202400 202400]]. This rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/FNBA_STAA8 FNBA_STAA8]] Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding site localized within the 17 C-terminal residues of the gamma-chain of human Fg. Both plasma proteins (Fn and Fg) function as a bridge between bacterium and host cell. Promotes attachment to immobilized elastin peptides in a dose-dependent and saturable manner. Promotes attachment to both full-length and segments of immobilized human tropoelastin at multiple sites in a dose and pH-dependent manner. Promotes adherence to and aggregation of activated platelets independently of other S.aureus surface molecules. Is a critical mediator implicated in the induction of experimental endocarditis in rats with catheter-induced aortic vegetations, promoting both colonization and persistence of the bacterium into the host.<ref>PMID:2521391</ref> <ref>PMID:10788510</ref> <ref>PMID:11736995</ref> <ref>PMID:11553573</ref> <ref>PMID:15234962</ref> <ref>PMID:15216468</ref> <ref>PMID:15897276</ref> <ref>PMID:17516661</ref> ~~[[https://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.~~		[https://www.uniprot.org/uniprot/FNBA_STAA8 FNBA_STAA8] Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding site localized within the 17 C-terminal residues of the gamma-chain of human Fg. Both plasma proteins (Fn and Fg) function as a bridge between bacterium and host cell. Promotes attachment to immobilized elastin peptides in a dose-dependent and saturable manner. Promotes attachment to both full-length and segments of immobilized human tropoelastin at multiple sites in a dose and pH-dependent manner. Promotes adherence to and aggregation of activated platelets independently of other S.aureus surface molecules. Is a critical mediator implicated in the induction of experimental endocarditis in rats with catheter-induced aortic vegetations, promoting both colonization and persistence of the bacterium into the host.<ref>PMID:2521391</ref> <ref>PMID:10788510</ref> <ref>PMID:11736995</ref> <ref>PMID:11553573</ref> <ref>PMID:15234962</ref> <ref>PMID:15216468</ref> <ref>PMID:15897276</ref> <ref>PMID:17516661</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Staa8~~]]		[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]]
	[[Category: Atkin~~, K E~~]]		[[Category: Atkin KE]]
	[[Category: Moroz, O]]		[[Category: Moroz O]]
	[[Category: Potts~~, J R~~]]		[[Category: Potts JR]]
	[[Category: Stemberk, V]]		[[Category: Stemberk V]]
	[[Category: Turkenburg~~, J P]]~~		[[Category: Turkenburg JP]]
	~~[[Category: Cell adhesion]]~~
	~~[[Category: Fibrinogen]]~~
	~~[[Category: Fibrinogen binding]]~~
	~~[[Category: Fnbpa~~]]

OCA at 07:00, 31 August 2022

2022-08-31T07:00:59Z

OCA at 13:26, 13 March 2019

2019-03-13T13:26:49Z

← Older revision		Revision as of 13:26, 13 March 2019
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	==Structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide==		==Structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide==
	<StructureSection load='4b60' size='340' side='right' caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>		<StructureSection load='4b60' size='340' side='right'caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4b60]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B60 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4b60]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B60 FirstGlance]. <br>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Staa8]]		[[Category: Staa8]]
	[[Category: Atkin, K E]]		[[Category: Atkin, K E]]

OCA at 18:05, 11 August 2016

2016-08-11T18:05:01Z

← Older revision		Revision as of 18:05, 11 August 2016
Line 1:		Line 1:

	==Structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide==		==Structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide==
	<StructureSection load='4b60' size='340' side='right' caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>		<StructureSection load='4b60' size='340' side='right' caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4b5z\|4b5z]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4b5z\|4b5z]]</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=4b60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b60 RCSB], [http://www.ebi.ac.uk/pdbsum/4b60 PDBsum]</span></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=4b60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b60 OCA], [http://pdbe.org/4b60 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b60 RCSB], [http://www.ebi.ac.uk/pdbsum/4b60 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b60 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4b60" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:53, 4 January 2015

2015-01-04T12:53:28Z

← Older revision		Revision as of 12:53, 4 January 2015
Line 2:		Line 2:
	<StructureSection load='4b60' size='340' side='right' caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>		<StructureSection load='4b60' size='340' side='right' caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4b60]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA]. <br>		<table><tr><td colspan='2'>[[4b60]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B60 FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4b5z\|4b5z]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4b5z\|4b5z]]</td></tr>
	<tr~~><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class~~='~~plainlinks~~'~~>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></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=4b60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b60 RCSB], [http://www.ebi.ac.uk/pdbsum/4b60 PDBsum]</span></td></tr>
	~~<tr~~><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b60 RCSB], [http://www.ebi.ac.uk/pdbsum/4b60 PDBsum]</span></td></tr>		</table>
	<table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Defects in FGG are a cause of congenital afibrinogenemia (CAFBN) [MIM:[http://omim.org/entry/202400 202400]]. This rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.		[[http://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Defects in FGG are a cause of congenital afibrinogenemia (CAFBN) [MIM:[http://omim.org/entry/202400 202400]]. This rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.
Line 18:		Line 17:
	Evidence for Steric Regulation of Fibrinogen binding to Staphylococcus aureus fibronectin-binding protein A (FnBPA).,Stemberk V, Jones RP, Moroz O, Atkin KE, Edwards AM, Turkenburg JP, Leech AP, Massey RC, Potts JR J Biol Chem. 2014 Mar 13. PMID:24627488<ref>PMID:24627488</ref>		Evidence for Steric Regulation of Fibrinogen binding to Staphylococcus aureus fibronectin-binding protein A (FnBPA).,Stemberk V, Jones RP, Moroz O, Atkin KE, Edwards AM, Turkenburg JP, Leech AP, Massey RC, Potts JR J Biol Chem. 2014 Mar 13. PMID:24627488<ref>PMID:24627488</ref>

	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==
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	</StructureSection>		</StructureSection>
	[[Category: Staa8]]		[[Category: Staa8]]
	[[Category: Atkin, K E.]]		[[Category: Atkin, K E]]
	[[Category: Moroz, O.]]		[[Category: Moroz, O]]
	[[Category: Potts, J R.]]		[[Category: Potts, J R]]
	[[Category: Stemberk, V.]]		[[Category: Stemberk, V]]
	[[Category: Turkenburg, J P.]]		[[Category: Turkenburg, J P]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]
	[[Category: Fibrinogen]]		[[Category: Fibrinogen]]
	[[Category: Fibrinogen binding]]		[[Category: Fibrinogen binding]]
	[[Category: Fnbpa]]		[[Category: Fnbpa]]

OCA at 06:59, 14 May 2014

2014-05-14T06:59:01Z

← Older revision		Revision as of 06:59, 14 May 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4b60\| PDB=4b60 \| SCENE= }}~~		==Structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide==
	===Structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide===		<StructureSection load='4b60' size='340' side='right' caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>
	~~{{ABSTRACT_PUBMED_24627488}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4b60]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA]. <br>
	==Disease==		</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4b5z\|4b5z]]</td></tr>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b60 RCSB], [http://www.ebi.ac.uk/pdbsum/4b60 PDBsum]</span></td></tr>
			<table>
			== Disease ==
	[[http://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Defects in FGG are a cause of congenital afibrinogenemia (CAFBN) [MIM:[http://omim.org/entry/202400 202400]]. This rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.		[[http://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Defects in FGG are a cause of congenital afibrinogenemia (CAFBN) [MIM:[http://omim.org/entry/202400 202400]]. This rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.
			== Function ==
	==Function==
	[[http://www.uniprot.org/uniprot/FNBA_STAA8 FNBA_STAA8]] Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding site localized within the 17 C-terminal residues of the gamma-chain of human Fg. Both plasma proteins (Fn and Fg) function as a bridge between bacterium and host cell. Promotes attachment to immobilized elastin peptides in a dose-dependent and saturable manner. Promotes attachment to both full-length and segments of immobilized human tropoelastin at multiple sites in a dose and pH-dependent manner. Promotes adherence to and aggregation of activated platelets independently of other S.aureus surface molecules. Is a critical mediator implicated in the induction of experimental endocarditis in rats with catheter-induced aortic vegetations, promoting both colonization and persistence of the bacterium into the host.<ref>PMID:2521391</ref> <ref>PMID:10788510</ref> <ref>PMID:11736995</ref> <ref>PMID:11553573</ref> <ref>PMID:15234962</ref> <ref>PMID:15216468</ref> <ref>PMID:15897276</ref> <ref>PMID:17516661</ref> [[http://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.		[[http://www.uniprot.org/uniprot/FNBA_STAA8 FNBA_STAA8]] Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding site localized within the 17 C-terminal residues of the gamma-chain of human Fg. Both plasma proteins (Fn and Fg) function as a bridge between bacterium and host cell. Promotes attachment to immobilized elastin peptides in a dose-dependent and saturable manner. Promotes attachment to both full-length and segments of immobilized human tropoelastin at multiple sites in a dose and pH-dependent manner. Promotes adherence to and aggregation of activated platelets independently of other S.aureus surface molecules. Is a critical mediator implicated in the induction of experimental endocarditis in rats with catheter-induced aortic vegetations, promoting both colonization and persistence of the bacterium into the host.<ref>PMID:2521391</ref> <ref>PMID:10788510</ref> <ref>PMID:11736995</ref> <ref>PMID:11553573</ref> <ref>PMID:15234962</ref> <ref>PMID:15216468</ref> <ref>PMID:15897276</ref> <ref>PMID:17516661</ref> [[http://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The adjacent fibrinogen (Fg)- and fibronectin (Fn)- binding sites on Fn-binding protein A (FnBPA), a cell-surface protein from Staphylococcus aureus, are implicated in the initiation and persistence of infection. FnBPA contains a single Fg-binding site (that also binds elastin) and multiple Fn-binding sites. Here, we solved the structure of the N2N3 domains containing the Fg-binding site of FnBPA in the apo-form and in complex with a Fg-peptide. The Fg-binding mechanism is similar to that of homologous bacterial proteins but without the requirement for latch strand residues. We show that the Fg- and the most N-terminal Fn-binding sites are non-overlapping but in close proximity. While Fg and a sub-domain of Fn can form a ternary complex on an FnBPA protein construct containing a Fg- and single Fn-binding site, binding of intact Fn appears to inhibit Fg binding, suggesting steric regulation. Given the concentrations of Fn and Fg in the plasma, this mechanism might result in targeting of S. aureus to fibrin-rich thrombi or elastin-rich tissues.

	~~==About this Structure==~~		Evidence for Steric Regulation of Fibrinogen binding to Staphylococcus aureus fibronectin-binding protein A (FnBPA).,Stemberk V, Jones RP, Moroz O, Atkin KE, Edwards AM, Turkenburg JP, Leech AP, Massey RC, Potts JR J Biol Chem. 2014 Mar 13. PMID:24627488<ref>PMID:24627488</ref>
	~~[[4b60]] is a 4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Staa8 Staa8]~~. ~~Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA].~~

	==~~Reference~~==		From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
	~~<ref group="xtra">PMID:024627488</ref>~~<references ~~group="xtra"~~/><~~references~~/>		</div>
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Staa8]]		[[Category: Staa8]]
	[[Category: Atkin, K E.]]		[[Category: Atkin, K E.]]

OCA at 08:08, 26 March 2014

2014-03-26T08:08:42Z

← Older revision		Revision as of 08:08, 26 March 2014
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	{{STRUCTURE_4b60\| PDB=4b60 \| SCENE= }}		{{STRUCTURE_4b60\| PDB=4b60 \| SCENE= }}
	===~~structure~~ of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide===		===Structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide===
			{{ABSTRACT_PUBMED_24627488}}

	==Disease==		==Disease==
Line 9:		Line 10:

	==About this Structure==		==About this Structure==
	[[4b60]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Staphylococcus_aureus_subsp._aureus_nctc_8325 Staphylococcus aureus subsp. aureus nctc 8325~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA].		[[4b60]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA].

	==Reference==		==Reference==
	<references group="xtra"/><references/>		<ref group="xtra">PMID:024627488</ref><references group="xtra"/><references/>
	[[Category: ~~Staphylococcus aureus subsp. aureus nctc 8325~~]]		[[Category: Staa8]]
	[[Category: Atkin, K E.]]		[[Category: Atkin, K E.]]
	[[Category: Moroz, O.]]		[[Category: Moroz, O.]]

OCA at 06:33, 10 October 2013

2013-10-10T06:33:59Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_4b60|  PDB=4b60  |  SCENE=  }}
-The entry 4b60 is ON HOLD  until Paper Publication
+==Disease==
-Authors: Stemberk, V., Moroz, O., Atkin, K.E., Turkenburg, J.P., Potts, J.R.
+==Function==
-Description: structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C-terminal peptide
+==About this Structure==

OCA at 04:35, 29 August 2012

2012-08-29T04:35:27Z

← Older revision		Revision as of 04:35, 29 August 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4b60 is ON HOLD		The entry 4b60 is ON HOLD until Paper Publication

	Authors: Stemberk, V., Moroz, O., Atkin, K.E., Turkenburg, J.P., Potts, J.R.		Authors: Stemberk, V., Moroz, O., Atkin, K.E., Turkenburg, J.P., Potts, J.R.

	Description: structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C-terminal peptide		Description: structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C-terminal peptide

OCA: Protected "4b60" [edit=sysop:move=sysop]

2012-08-15T05:12:57Z

Protected "4b60" [edit=sysop:move=sysop]

← Older revision	Revision as of 05:12, 15 August 2012
(No difference)

← Older revision		Revision as of 07:00, 31 August 2022
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	<StructureSection load='4b60' size='340' side='right'caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>		<StructureSection load='4b60' size='340' side='right'caption='[[4b60]], [[Resolution\|resolution]] 1.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4b60]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4B60 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4b60]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B60 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4b5z\|4b5z]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b5z\|4b5z]]</div></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=4b60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b60 OCA], [~~http~~://pdbe.org/4b60 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4b60 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4b60 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4b60 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=4b60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b60 OCA], [https://pdbe.org/4b60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b60 RCSB], [https://www.ebi.ac.uk/pdbsum/4b60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b60 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Defects in FGG are a cause of congenital afibrinogenemia (CAFBN) [MIM:[~~http~~://omim.org/entry/202400 202400]]. This rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.		[[https://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Defects in FGG are a cause of congenital afibrinogenemia (CAFBN) [MIM:[https://omim.org/entry/202400 202400]]. This rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/FNBA_STAA8 FNBA_STAA8]] Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding site localized within the 17 C-terminal residues of the gamma-chain of human Fg. Both plasma proteins (Fn and Fg) function as a bridge between bacterium and host cell. Promotes attachment to immobilized elastin peptides in a dose-dependent and saturable manner. Promotes attachment to both full-length and segments of immobilized human tropoelastin at multiple sites in a dose and pH-dependent manner. Promotes adherence to and aggregation of activated platelets independently of other S.aureus surface molecules. Is a critical mediator implicated in the induction of experimental endocarditis in rats with catheter-induced aortic vegetations, promoting both colonization and persistence of the bacterium into the host.<ref>PMID:2521391</ref> <ref>PMID:10788510</ref> <ref>PMID:11736995</ref> <ref>PMID:11553573</ref> <ref>PMID:15234962</ref> <ref>PMID:15216468</ref> <ref>PMID:15897276</ref> <ref>PMID:17516661</ref> [[~~http~~://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.		[[https://www.uniprot.org/uniprot/FNBA_STAA8 FNBA_STAA8]] Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding site localized within the 17 C-terminal residues of the gamma-chain of human Fg. Both plasma proteins (Fn and Fg) function as a bridge between bacterium and host cell. Promotes attachment to immobilized elastin peptides in a dose-dependent and saturable manner. Promotes attachment to both full-length and segments of immobilized human tropoelastin at multiple sites in a dose and pH-dependent manner. Promotes adherence to and aggregation of activated platelets independently of other S.aureus surface molecules. Is a critical mediator implicated in the induction of experimental endocarditis in rats with catheter-induced aortic vegetations, promoting both colonization and persistence of the bacterium into the host.<ref>PMID:2521391</ref> <ref>PMID:10788510</ref> <ref>PMID:11736995</ref> <ref>PMID:11553573</ref> <ref>PMID:15234962</ref> <ref>PMID:15216468</ref> <ref>PMID:15897276</ref> <ref>PMID:17516661</ref> [[https://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN]] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==