1ivc - Revision history

OCA at 07:49, 3 April 2024

OCA — Wed, 03 Apr 2024 07:49:11 GMT

←Older revision		Revision as of 07:49, 3 April 2024
Line 3:		Line 3:
	<StructureSection load='1ivc' size='340' side='right'caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1ivc' size='340' side='right'caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~I67a0 I67a0~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IVC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Tokyo/3/1967(H2N2)) Influenza A virus (A/Tokyo/3/1967(H2N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IVC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA~~</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2~~</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.4Å</td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exo~~-~~alpha~~-~~sialidase Exo~~-~~alpha~~-~~sialidase], with EC number [https://www.brenda~~-~~enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2</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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [https://pdbe.org/1ivc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [https://www.ebi.ac.uk/pdbsum/1ivc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ivc 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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [https://pdbe.org/1ivc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [https://www.ebi.ac.uk/pdbsum/1ivc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ivc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/NRAM_I67A0 NRAM_I67A0]] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.	+	[https://www.uniprot.org/uniprot/NRAM_I67A0 NRAM_I67A0] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</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=1ivc ConSurf].		</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=1ivc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Neuraminidase (NA), a surface glycoprotein of influenza virus, is a potential target for design of antiinfluenza agents. The crystal structure of influenza virus neuraminidase showed that in the active site 11 residues are universally conserved among all strains known so far. Several potent inhibitors based on the carbohydrate compound 2-deoxy-2,3-didehydro-D-N-acetylneuraminic acid (DANA) have been shown to bind to the conserved active site and to reduce virus infection in animals when administered by nasal spray. Inhibitors of this type are, however, rapidly excreted from physiological systems and may not be effective in order to provide long-time protection. A new class of specific NA inhibitors, which are benzoic acid derivatives, has been designed on the basis of the three-dimensional structure of the NA-DANA complex and modeling of derivatives of 4-(acetylamino)benzoic acid in the NA active site. Intermediates were synthesized and were shown to moderately inhibit the NA activity and to bind to the NA active site as predicted. These rudimentary inhibitors, 4-(acetylamino)-3-hydroxy-5-nitrobenzoic acid, 4-(acetylamino)-3-hydroxy-5-aminobenzoic acid, and 4-(acetylamino)-3-aminobenzoic acid, and their X-ray structures in complexes with N2 (A/Tokyo/3/67) and B/Lee/40 neuraminidases have been analyzed. The coordinates of such inhibitors complexed with NA were used as the starting model for further design of more potent benzoic acid inhibitors. Because the active site residues of NA are invariant, the designed aromatic inhibitors have the potential to become an antiviral drug against all strains of influenza virus.
-
-	Structures of aromatic inhibitors of influenza virus neuraminidase.,Jedrzejas MJ, Singh S, Brouillette WJ, Laver WG, Air GM, Luo M Biochemistry. 1995 Mar 14;34(10):3144-51. PMID:7880809<ref>PMID:7880809</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1ivc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Neuraminidase 3D structures\|Neuraminidase 3D structures]]		*[[Neuraminidase 3D structures\|Neuraminidase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Exo-alpha-sialidase]]
-	[[Category: I67a0]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Jedrzejas~~, M J~~]]	+	[[Category: Jedrzejas MJ]]
-	[[Category: Luo, M]]	+	[[Category: Luo M]]

OCA at 07:14, 14 April 2021

OCA — Wed, 14 Apr 2021 07:14:23 GMT

←Older revision		Revision as of 07:14, 14 April 2021
Line 3:		Line 3:
	<StructureSection load='1ivc' size='340' side='right'caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1ivc' size='340' side='right'caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/I67a0 I67a0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1IVC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/I67a0 I67a0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IVC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG~~</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2~~</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [~~http~~://pdbe.org/1ivc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1ivc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1ivc 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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [https://pdbe.org/1ivc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [https://www.ebi.ac.uk/pdbsum/1ivc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ivc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/NRAM_I67A0 NRAM_I67A0]] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.	+	[[https://www.uniprot.org/uniprot/NRAM_I67A0 NRAM_I67A0]] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Neuraminidase\|Neuraminidase]]	+	*[[Neuraminidase 3D structures\|Neuraminidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:23, 10 July 2019

OCA — Wed, 10 Jul 2019 07:23:25 GMT

←Older revision		Revision as of 07:23, 10 July 2019
Line 1:		Line 1:

	==STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE==		==STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE==
-	<StructureSection load='1ivc' size='340' side='right' caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='1ivc' size='340' side='right'caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/I67a0 I67a0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVC FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/I67a0 I67a0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVC FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iv/1ivc_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iv/1ivc_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 38:		Line 38:
	[[Category: Exo-alpha-sialidase]]		[[Category: Exo-alpha-sialidase]]
	[[Category: I67a0]]		[[Category: I67a0]]
		+	[[Category: Large Structures]]
	[[Category: Jedrzejas, M J]]		[[Category: Jedrzejas, M J]]
	[[Category: Luo, M]]		[[Category: Luo, M]]

OCA at 09:53, 4 October 2017

OCA — Wed, 04 Oct 2017 09:53:52 GMT

←Older revision		Revision as of 09:53, 4 October 2017
Line 1:		Line 1:
		+
	==STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE==		==STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE==
	<StructureSection load='1ivc' size='340' side='right' caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1ivc' size='340' side='right' caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/I67a0 I67a0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVC FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/I67a0 I67a0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA~~</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2~~</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [http://pdbe.org/1ivc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [http://www.ebi.ac.uk/pdbsum/1ivc 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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [http://pdbe.org/1ivc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [http://www.ebi.ac.uk/pdbsum/1ivc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ivc ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=1ivc ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 14:06, 11 September 2015

OCA — Fri, 11 Sep 2015 14:06:17 GMT

←Older revision		Revision as of 14:06, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1ivc' size='340' side='right' caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='1ivc' size='340' side='right' caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Influenza_a_virus_(a/tokyo/3/1967(h2n2)) Influenza a virus (a/tokyo/3/1967(h2n2))~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/I67a0 I67a0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVC FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [http://www.ebi.ac.uk/pdbsum/1ivc 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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [http://pdbe.org/1ivc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [http://www.ebi.ac.uk/pdbsum/1ivc PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	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 1ivc" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Exo-alpha-sialidase]]		[[Category: Exo-alpha-sialidase]]
		+	[[Category: I67a0]]
	[[Category: Jedrzejas, M J]]		[[Category: Jedrzejas, M J]]
	[[Category: Luo, M]]		[[Category: Luo, M]]

OCA at 17:29, 25 December 2014

OCA — Thu, 25 Dec 2014 17:29:25 GMT

←Older revision		Revision as of 17:29, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/tokyo/3/1967(h2n2)) Influenza a virus (a/tokyo/3/1967(h2n2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVC FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/tokyo/3/1967(h2n2)) Influenza a virus (a/tokyo/3/1967(h2n2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVC FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [http://www.ebi.ac.uk/pdbsum/1ivc 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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [http://www.ebi.ac.uk/pdbsum/1ivc PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NRAM_I67A0 NRAM_I67A0]] Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Exo-alpha-sialidase]]		[[Category: Exo-alpha-sialidase]]
-	[[Category: Jedrzejas, M J.]]	+	[[Category: Jedrzejas, M J]]
-	[[Category: Luo, M.]]	+	[[Category: Luo, M]]

OCA at 12:13, 28 September 2014

OCA — Sun, 28 Sep 2014 12:13:32 GMT

←Older revision		Revision as of 12:13, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1ivc.~~png\|left~~\|200px]]	+	==STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE==
		+	<StructureSection load='1ivc' size='340' side='right' caption='[[1ivc]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1ivc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/tokyo/3/1967(h2n2)) Influenza a virus (a/tokyo/3/1967(h2n2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVC FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ST2:4-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC+ACID'>ST2</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=1ivc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ivc RCSB], [http://www.ebi.ac.uk/pdbsum/1ivc PDBsum]</span></td></tr>
		+	<table>
		+	== 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/iv/1ivc_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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Neuraminidase (NA), a surface glycoprotein of influenza virus, is a potential target for design of antiinfluenza agents. The crystal structure of influenza virus neuraminidase showed that in the active site 11 residues are universally conserved among all strains known so far. Several potent inhibitors based on the carbohydrate compound 2-deoxy-2,3-didehydro-D-N-acetylneuraminic acid (DANA) have been shown to bind to the conserved active site and to reduce virus infection in animals when administered by nasal spray. Inhibitors of this type are, however, rapidly excreted from physiological systems and may not be effective in order to provide long-time protection. A new class of specific NA inhibitors, which are benzoic acid derivatives, has been designed on the basis of the three-dimensional structure of the NA-DANA complex and modeling of derivatives of 4-(acetylamino)benzoic acid in the NA active site. Intermediates were synthesized and were shown to moderately inhibit the NA activity and to bind to the NA active site as predicted. These rudimentary inhibitors, 4-(acetylamino)-3-hydroxy-5-nitrobenzoic acid, 4-(acetylamino)-3-hydroxy-5-aminobenzoic acid, and 4-(acetylamino)-3-aminobenzoic acid, and their X-ray structures in complexes with N2 (A/Tokyo/3/67) and B/Lee/40 neuraminidases have been analyzed. The coordinates of such inhibitors complexed with NA were used as the starting model for further design of more potent benzoic acid inhibitors. Because the active site residues of NA are invariant, the designed aromatic inhibitors have the potential to become an antiviral drug against all strains of influenza virus.

-	~~{{STRUCTURE_1ivc\| PDB=1ivc \| SCENE= }}~~	+	Structures of aromatic inhibitors of influenza virus neuraminidase.,Jedrzejas MJ, Singh S, Brouillette WJ, Laver WG, Air GM, Luo M Biochemistry. 1995 Mar 14;34(10):3144-51. PMID:7880809<ref>PMID:7880809</ref>

-	~~===STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_7880809}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[1ivc]] is a 2 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Influenza_a_virus_(~~a~~/tokyo/3/1967(h2n2)) Influenza a virus (a/tokyo/3/1967(h2n2))]~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=1IVC OCA].~~	+

	==See Also==		==See Also==
	*[[Neuraminidase\|Neuraminidase]]		*[[Neuraminidase\|Neuraminidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:007880809<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Exo-alpha-sialidase]]		[[Category: Exo-alpha-sialidase]]
	[[Category: Jedrzejas, M J.]]		[[Category: Jedrzejas, M J.]]
	[[Category: Luo, M.]]		[[Category: Luo, M.]]

OCA at 19:27, 20 October 2012

OCA — Sat, 20 Oct 2012 19:27:24 GMT

←Older revision		Revision as of 19:27, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1ivc]] is a 2 chain structure ~~of [[Neuraminidase]]~~ with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(~~strain_a~~/tokyo/3/~~1967_h2n2~~) Influenza a virus (~~strain~~ a/tokyo/3/1967 h2n2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA].	+	[[1ivc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/tokyo/3/1967(h2n2)) Influenza a virus (a/tokyo/3/1967(h2n2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA].

	==See Also==		==See Also==

OCA: Protected "1ivc" [edit=sysop:move=sysop]

OCA — Fri, 27 Jul 2012 07:24:38 GMT

Protected "1ivc" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:24, 27 July 2012

OCA at 07:24, 27 July 2012

OCA — Fri, 27 Jul 2012 07:24:37 GMT

←Older revision		Revision as of 07:24, 27 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1ivc.png\|left\|200px]]		[[Image:1ivc.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1ivc", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1ivc\| PDB=1ivc \| SCENE= }}		{{STRUCTURE_1ivc\| PDB=1ivc \| SCENE= }}

	===STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE===		===STRUCTURES OF AROMATIC INHIBITORS OF INFLUENZA VIRUS NEURAMINIDASE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_7880809}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 7880809 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_7880809}}		{{ABSTRACT_PUBMED_7880809}}

	==About this Structure==		==About this Structure==
-	~~1IVC~~ is a 2 ~~chains~~ structure of ~~sequences~~ from [http://en.wikipedia.org/wiki/Influenza_a_virus_(strain_a/tokyo/3/1967_h2n2) Influenza a virus (strain a/tokyo/3/1967 h2n2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA].	+	[[1ivc]] is a 2 chain structure of [[Neuraminidase]] with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(strain_a/tokyo/3/1967_h2n2) Influenza a virus (strain a/tokyo/3/1967 h2n2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVC OCA].
		+
		+	==See Also==
		+	*[[Neuraminidase\|Neuraminidase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~7880809~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:007880809</ref><references group="xtra"/>
	[[Category: Exo-alpha-sialidase]]		[[Category: Exo-alpha-sialidase]]
	[[Category: Jedrzejas, M J.]]		[[Category: Jedrzejas, M J.]]
	[[Category: Luo, M.]]		[[Category: Luo, M.]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 21 19:41:48 2009''