2vdp - Revision history

OCA at 07:58, 4 November 2020

OCA — Wed, 04 Nov 2020 07:58:16 GMT

←Older revision		Revision as of 07:58, 4 November 2020
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	==Integrin AlphaIIbBeta3 Headpiece Bound to Fibrinogen Gamma chain peptide,LGGAKQAGDV==		==Integrin AlphaIIbBeta3 Headpiece Bound to Fibrinogen Gamma chain peptide,LGGAKQAGDV==
-	<StructureSection load='2vdp' size='340' side='right' caption='[[2vdp]], [[Resolution\|resolution]] 2.80Å' scene=''>	+	<StructureSection load='2vdp' size='340' side='right'caption='[[2vdp]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vdp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=2VDP OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2VDP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vdp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=2VDP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VDP 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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=~~MAN~~:~~ALPHA-D-MANNOSE~~'>~~MAN~~</scene>, <scene name='pdbligand=MG:~~MAGNESIUM+ION~~'>MG</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" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mk7\|1mk7]], [[2vdq\|2vdq]], [[1m8o\|1m8o]], [[1s4x\|1s4x]], [[2vdn\|2vdn]], [[1uv9\|1uv9]], [[1tye\|1tye]], [[1s4w\|1s4w]], [[1mk9\|1mk9]], [[1m1x\|1m1x]], [[1rn0\|1rn0]], [[1l5g\|1l5g]], [[2vdm\|2vdm]], [[1dpq\|1dpq]], [[2vdo\|2vdo]], [[1jv2\|1jv2]], [[1dpk\|1dpk]], [[2vdr\|2vdr]], [[2vdk\|2vdk]], [[1kup\|1kup]], [[1kuz\|1kuz]], [[2vdl\|2vdl]], [[1miz\|1miz]], [[1u8c\|1u8c]], [[1jx5\|1jx5]], [[2vc2\|2vc2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mk7\|1mk7]], [[2vdq\|2vdq]], [[1m8o\|1m8o]], [[1s4x\|1s4x]], [[2vdn\|2vdn]], [[1uv9\|1uv9]], [[1tye\|1tye]], [[1s4w\|1s4w]], [[1mk9\|1mk9]], [[1m1x\|1m1x]], [[1rn0\|1rn0]], [[1l5g\|1l5g]], [[2vdm\|2vdm]], [[1dpq\|1dpq]], [[2vdo\|2vdo]], [[1jv2\|1jv2]], [[1dpk\|1dpk]], [[2vdr\|2vdr]], [[2vdk\|2vdk]], [[1kup\|1kup]], [[1kuz\|1kuz]], [[2vdl\|2vdl]], [[1miz\|1miz]], [[1u8c\|1u8c]], [[1jx5\|1jx5]], [[2vc2\|2vc2]]</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=2vdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdp OCA], [http://pdbe.org/2vdp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vdp RCSB], [http://www.ebi.ac.uk/pdbsum/2vdp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vdp ProSAT]</span></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=2vdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdp OCA], [http://pdbe.org/2vdp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vdp RCSB], [http://www.ebi.ac.uk/pdbsum/2vdp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vdp ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 34:		Line 34:
	==See Also==		==See Also==
	*[[Fibrinogen\|Fibrinogen]]		*[[Fibrinogen\|Fibrinogen]]
-	*[[Integrin\|Integrin]]	+	*[[Integrin 3D structures\|Integrin 3D structures]]
	*[[Monoclonal Antibodies 3D structures\|Monoclonal Antibodies 3D structures]]		*[[Monoclonal Antibodies 3D structures\|Monoclonal Antibodies 3D structures]]
	== References ==		== References ==
Line 41:		Line 41:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Springer, T A]]		[[Category: Springer, T A]]

OCA at 20:41, 19 September 2018

OCA — Wed, 19 Sep 2018 20:41:20 GMT

←Older revision		Revision as of 20:41, 19 September 2018
Line 1:		Line 1:
-	==~~INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO FIBRINOGEN GAMMA CHAIN PEPTIDE~~,LGGAKQAGDV==	+
		+	==Integrin AlphaIIbBeta3 Headpiece Bound to Fibrinogen Gamma chain peptide,LGGAKQAGDV==
	<StructureSection load='2vdp' size='340' side='right' caption='[[2vdp]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='2vdp' size='340' side='right' caption='[[2vdp]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vdp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=2VDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VDP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vdp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=2VDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VDP 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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:~~MAGNESIUM+ION~~'>MG</scene>, <scene name='pdbligand=~~NAG~~:~~N-ACETYL-D-GLUCOSAMINE~~'>~~NAG~~</scene>, <scene name='pdbligand=~~MAN~~:~~ALPHA~~-D-~~MANNOSE~~'>~~MAN~~</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mk7\|1mk7]], [[2vdq\|2vdq]], [[1m8o\|1m8o]], [[1s4x\|1s4x]], [[2vdn\|2vdn]], [[1uv9\|1uv9]], [[1tye\|1tye]], [[1s4w\|1s4w]], [[1mk9\|1mk9]], [[1m1x\|1m1x]], [[1rn0\|1rn0]], [[1l5g\|1l5g]], [[2vdm\|2vdm]], [[1dpq\|1dpq]], [[2vdo\|2vdo]], [[1jv2\|1jv2]], [[1dpk\|1dpk]], [[2vdr\|2vdr]], [[2vdk\|2vdk]], [[1kup\|1kup]], [[1kuz\|1kuz]], [[2vdl\|2vdl]], [[1miz\|1miz]], [[1u8c\|1u8c]], [[1jx5\|1jx5]], [[2vc2\|2vc2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mk7\|1mk7]], [[2vdq\|2vdq]], [[1m8o\|1m8o]], [[1s4x\|1s4x]], [[2vdn\|2vdn]], [[1uv9\|1uv9]], [[1tye\|1tye]], [[1s4w\|1s4w]], [[1mk9\|1mk9]], [[1m1x\|1m1x]], [[1rn0\|1rn0]], [[1l5g\|1l5g]], [[2vdm\|2vdm]], [[1dpq\|1dpq]], [[2vdo\|2vdo]], [[1jv2\|1jv2]], [[1dpk\|1dpk]], [[2vdr\|2vdr]], [[2vdk\|2vdk]], [[1kup\|1kup]], [[1kuz\|1kuz]], [[2vdl\|2vdl]], [[1miz\|1miz]], [[1u8c\|1u8c]], [[1jx5\|1jx5]], [[2vc2\|2vc2]]</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=2vdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdp OCA], [http://pdbe.org/2vdp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vdp RCSB], [http://www.ebi.ac.uk/pdbsum/2vdp 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=2vdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdp OCA], [http://pdbe.org/2vdp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vdp RCSB], [http://www.ebi.ac.uk/pdbsum/2vdp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vdp ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 15:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vd/2vdp_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vd/2vdp_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 34:		Line 35:
	*[[Fibrinogen\|Fibrinogen]]		*[[Fibrinogen\|Fibrinogen]]
	*[[Integrin\|Integrin]]		*[[Integrin\|Integrin]]
-	*[[Monoclonal ~~Antibody~~\|Monoclonal ~~Antibody~~]]	+	*[[Monoclonal Antibodies 3D structures\|Monoclonal Antibodies 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:26, 7 February 2016

OCA — Sun, 07 Feb 2016 16:26:31 GMT

←Older revision		Revision as of 16:26, 7 February 2016
Line 2:		Line 2:
	<StructureSection load='2vdp' size='340' side='right' caption='[[2vdp]], [[Resolution\|resolution]] 2.80Å' scene=''>		<StructureSection load='2vdp' size='340' side='right' caption='[[2vdp]], [[Resolution\|resolution]] 2.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2vdp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~] 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=2VDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VDP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2vdp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] 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=2VDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VDP 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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mk7\|1mk7]], [[2vdq\|2vdq]], [[1m8o\|1m8o]], [[1s4x\|1s4x]], [[2vdn\|2vdn]], [[1uv9\|1uv9]], [[1tye\|1tye]], [[1s4w\|1s4w]], [[1mk9\|1mk9]], [[1m1x\|1m1x]], [[1rn0\|1rn0]], [[1l5g\|1l5g]], [[2vdm\|2vdm]], [[1dpq\|1dpq]], [[2vdo\|2vdo]], [[1jv2\|1jv2]], [[1dpk\|1dpk]], [[2vdr\|2vdr]], [[2vdk\|2vdk]], [[1kup\|1kup]], [[1kuz\|1kuz]], [[2vdl\|2vdl]], [[1miz\|1miz]], [[1u8c\|1u8c]], [[1jx5\|1jx5]], [[2vc2\|2vc2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mk7\|1mk7]], [[2vdq\|2vdq]], [[1m8o\|1m8o]], [[1s4x\|1s4x]], [[2vdn\|2vdn]], [[1uv9\|1uv9]], [[1tye\|1tye]], [[1s4w\|1s4w]], [[1mk9\|1mk9]], [[1m1x\|1m1x]], [[1rn0\|1rn0]], [[1l5g\|1l5g]], [[2vdm\|2vdm]], [[1dpq\|1dpq]], [[2vdo\|2vdo]], [[1jv2\|1jv2]], [[1dpk\|1dpk]], [[2vdr\|2vdr]], [[2vdk\|2vdk]], [[1kup\|1kup]], [[1kuz\|1kuz]], [[2vdl\|2vdl]], [[1miz\|1miz]], [[1u8c\|1u8c]], [[1jx5\|1jx5]], [[2vc2\|2vc2]]</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=2vdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vdp RCSB], [http://www.ebi.ac.uk/pdbsum/2vdp 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=2vdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdp OCA], [http://pdbe.org/2vdp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vdp RCSB], [http://www.ebi.ac.uk/pdbsum/2vdp PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Defects in ITGA2B are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:8282784</ref> <ref>PMID:7508443</ref> <ref>PMID:7706461</ref> <ref>PMID:8704171</ref> <ref>PMID:9215749</ref> <ref>PMID:9473221</ref> <ref>PMID:9763559</ref> <ref>PMID:9722314</ref> <ref>PMID:9734640</ref> <ref>PMID:9920835</ref> <ref>PMID:10607701</ref> <ref>PMID:11798398</ref> <ref>PMID:12181054</ref> <ref>PMID:12083483</ref> <ref>PMID:12424194</ref> <ref>PMID:12506038</ref> <ref>PMID:15099289</ref> <ref>PMID:15219201</ref> <ref>PMID:17018384</ref> [[http://www.uniprot.org/uniprot/ITB3_HUMAN ITB3_HUMAN]] Defects in ITGB3 are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:2392682</ref> <ref>PMID:1371279</ref> <ref>PMID:1602006</ref> <ref>PMID:1438206</ref> <ref>PMID:8781422</ref> <ref>PMID:9376589</ref> <ref>PMID:9215749</ref> <ref>PMID:9790984</ref> <ref>PMID:9684783</ref> <ref>PMID:10233432</ref> <ref>PMID:11588040</ref> <ref>PMID:11897046</ref> <ref>PMID:12083483</ref> <ref>PMID:12353082</ref> <ref>PMID:15583747</ref> <ref>PMID:15634267</ref> <ref>PMID:15748237</ref>	+	[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Defects in ITGA2B are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:8282784</ref> <ref>PMID:7508443</ref> <ref>PMID:7706461</ref> <ref>PMID:8704171</ref> <ref>PMID:9215749</ref> <ref>PMID:9473221</ref> <ref>PMID:9763559</ref> <ref>PMID:9722314</ref> <ref>PMID:9734640</ref> <ref>PMID:9920835</ref> <ref>PMID:10607701</ref> <ref>PMID:11798398</ref> <ref>PMID:12181054</ref> <ref>PMID:12083483</ref> <ref>PMID:12424194</ref> <ref>PMID:12506038</ref> <ref>PMID:15099289</ref> <ref>PMID:15219201</ref> <ref>PMID:17018384</ref> [[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/ITB3_HUMAN ITB3_HUMAN]] Defects in ITGB3 are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:2392682</ref> <ref>PMID:1371279</ref> <ref>PMID:1602006</ref> <ref>PMID:1438206</ref> <ref>PMID:8781422</ref> <ref>PMID:9376589</ref> <ref>PMID:9215749</ref> <ref>PMID:9790984</ref> <ref>PMID:9684783</ref> <ref>PMID:10233432</ref> <ref>PMID:11588040</ref> <ref>PMID:11897046</ref> <ref>PMID:12083483</ref> <ref>PMID:12353082</ref> <ref>PMID:15583747</ref> <ref>PMID:15634267</ref> <ref>PMID:15748237</ref>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface. [[http://www.uniprot.org/uniprot/ITB3_HUMAN ITB3_HUMAN]] Integrin alpha-V/beta-3 is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.	+	[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface. [[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/ITB3_HUMAN ITB3_HUMAN]] Integrin alpha-V/beta-3 is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		Line 19:
	<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=2vdp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 29:		Line 29:
	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 2vdp" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 39:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Springer, T A]]		[[Category: Springer, T A]]

OCA at 17:25, 19 January 2015

OCA — Mon, 19 Jan 2015 17:25:34 GMT

←Older revision		Revision as of 17:25, 19 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vdp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=2VDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VDP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vdp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=2VDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VDP FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mk7\|1mk7]], [[2vdq\|2vdq]], [[1m8o\|1m8o]], [[1s4x\|1s4x]], [[2vdn\|2vdn]], [[1uv9\|1uv9]], [[1tye\|1tye]], [[1s4w\|1s4w]], [[1mk9\|1mk9]], [[1m1x\|1m1x]], [[1rn0\|1rn0]], [[1l5g\|1l5g]], [[2vdm\|2vdm]], [[1dpq\|1dpq]], [[2vdo\|2vdo]], [[1jv2\|1jv2]], [[1dpk\|1dpk]], [[2vdr\|2vdr]], [[2vdk\|2vdk]], [[1kup\|1kup]], [[1kuz\|1kuz]], [[2vdl\|2vdl]], [[1miz\|1miz]], [[1u8c\|1u8c]], [[1jx5\|1jx5]], [[2vc2\|2vc2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mk7\|1mk7]], [[2vdq\|2vdq]], [[1m8o\|1m8o]], [[1s4x\|1s4x]], [[2vdn\|2vdn]], [[1uv9\|1uv9]], [[1tye\|1tye]], [[1s4w\|1s4w]], [[1mk9\|1mk9]], [[1m1x\|1m1x]], [[1rn0\|1rn0]], [[1l5g\|1l5g]], [[2vdm\|2vdm]], [[1dpq\|1dpq]], [[2vdo\|2vdo]], [[1jv2\|1jv2]], [[1dpk\|1dpk]], [[2vdr\|2vdr]], [[2vdk\|2vdk]], [[1kup\|1kup]], [[1kuz\|1kuz]], [[2vdl\|2vdl]], [[1miz\|1miz]], [[1u8c\|1u8c]], [[1jx5\|1jx5]], [[2vc2\|2vc2]]</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=2vdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vdp RCSB], [http://www.ebi.ac.uk/pdbsum/2vdp 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=2vdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vdp RCSB], [http://www.ebi.ac.uk/pdbsum/2vdp PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Defects in ITGA2B are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:8282784</ref> <ref>PMID:7508443</ref> <ref>PMID:7706461</ref> <ref>PMID:8704171</ref> <ref>PMID:9215749</ref> <ref>PMID:9473221</ref> <ref>PMID:9763559</ref> <ref>PMID:9722314</ref> <ref>PMID:9734640</ref> <ref>PMID:9920835</ref> <ref>PMID:10607701</ref> <ref>PMID:11798398</ref> <ref>PMID:12181054</ref> <ref>PMID:12083483</ref> <ref>PMID:12424194</ref> <ref>PMID:12506038</ref> <ref>PMID:15099289</ref> <ref>PMID:15219201</ref> <ref>PMID:17018384</ref> [[http://www.uniprot.org/uniprot/ITB3_HUMAN ITB3_HUMAN]] Defects in ITGB3 are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:2392682</ref> <ref>PMID:1371279</ref> <ref>PMID:1602006</ref> <ref>PMID:1438206</ref> <ref>PMID:8781422</ref> <ref>PMID:9376589</ref> <ref>PMID:9215749</ref> <ref>PMID:9790984</ref> <ref>PMID:9684783</ref> <ref>PMID:10233432</ref> <ref>PMID:11588040</ref> <ref>PMID:11897046</ref> <ref>PMID:12083483</ref> <ref>PMID:12353082</ref> <ref>PMID:15583747</ref> <ref>PMID:15634267</ref> <ref>PMID:15748237</ref>		[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Defects in ITGA2B are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:8282784</ref> <ref>PMID:7508443</ref> <ref>PMID:7706461</ref> <ref>PMID:8704171</ref> <ref>PMID:9215749</ref> <ref>PMID:9473221</ref> <ref>PMID:9763559</ref> <ref>PMID:9722314</ref> <ref>PMID:9734640</ref> <ref>PMID:9920835</ref> <ref>PMID:10607701</ref> <ref>PMID:11798398</ref> <ref>PMID:12181054</ref> <ref>PMID:12083483</ref> <ref>PMID:12424194</ref> <ref>PMID:12506038</ref> <ref>PMID:15099289</ref> <ref>PMID:15219201</ref> <ref>PMID:17018384</ref> [[http://www.uniprot.org/uniprot/ITB3_HUMAN ITB3_HUMAN]] Defects in ITGB3 are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:2392682</ref> <ref>PMID:1371279</ref> <ref>PMID:1602006</ref> <ref>PMID:1438206</ref> <ref>PMID:8781422</ref> <ref>PMID:9376589</ref> <ref>PMID:9215749</ref> <ref>PMID:9790984</ref> <ref>PMID:9684783</ref> <ref>PMID:10233432</ref> <ref>PMID:11588040</ref> <ref>PMID:11897046</ref> <ref>PMID:12083483</ref> <ref>PMID:12353082</ref> <ref>PMID:15583747</ref> <ref>PMID:15634267</ref> <ref>PMID:15748237</ref>
Line 40:		Line 40:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Springer, T A.]]	+	[[Category: Springer, T A]]
-	[[Category: Xiao, T.]]	+	[[Category: Xiao, T]]
-	[[Category: Zhu, J.]]	+	[[Category: Zhu, J]]
	[[Category: Antagonist]]		[[Category: Antagonist]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]

OCA at 01:53, 1 October 2014

OCA — Wed, 01 Oct 2014 01:53:30 GMT

←Older revision		Revision as of 01:53, 1 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2vdp\| PDB=2vdp \| SCENE= }}~~	+	==INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV==
-	===INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV===	+	<StructureSection load='2vdp' size='340' side='right' caption='[[2vdp]], [[Resolution\|resolution]] 2.80Å' scene=''>
-	~~{{ABSTRACT_PUBMED_18710925}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2vdp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=2VDP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VDP FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1mk7\|1mk7]], [[2vdq\|2vdq]], [[1m8o\|1m8o]], [[1s4x\|1s4x]], [[2vdn\|2vdn]], [[1uv9\|1uv9]], [[1tye\|1tye]], [[1s4w\|1s4w]], [[1mk9\|1mk9]], [[1m1x\|1m1x]], [[1rn0\|1rn0]], [[1l5g\|1l5g]], [[2vdm\|2vdm]], [[1dpq\|1dpq]], [[2vdo\|2vdo]], [[1jv2\|1jv2]], [[1dpk\|1dpk]], [[2vdr\|2vdr]], [[2vdk\|2vdk]], [[1kup\|1kup]], [[1kuz\|1kuz]], [[2vdl\|2vdl]], [[1miz\|1miz]], [[1u8c\|1u8c]], [[1jx5\|1jx5]], [[2vc2\|2vc2]]</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=2vdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vdp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vdp RCSB], [http://www.ebi.ac.uk/pdbsum/2vdp PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Defects in ITGA2B are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:8282784</ref> <ref>PMID:7508443</ref> <ref>PMID:7706461</ref> <ref>PMID:8704171</ref> <ref>PMID:9215749</ref> <ref>PMID:9473221</ref> <ref>PMID:9763559</ref> <ref>PMID:9722314</ref> <ref>PMID:9734640</ref> <ref>PMID:9920835</ref> <ref>PMID:10607701</ref> <ref>PMID:11798398</ref> <ref>PMID:12181054</ref> <ref>PMID:12083483</ref> <ref>PMID:12424194</ref> <ref>PMID:12506038</ref> <ref>PMID:15099289</ref> <ref>PMID:15219201</ref> <ref>PMID:17018384</ref> [[http://www.uniprot.org/uniprot/ITB3_HUMAN ITB3_HUMAN]] Defects in ITGB3 are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:2392682</ref> <ref>PMID:1371279</ref> <ref>PMID:1602006</ref> <ref>PMID:1438206</ref> <ref>PMID:8781422</ref> <ref>PMID:9376589</ref> <ref>PMID:9215749</ref> <ref>PMID:9790984</ref> <ref>PMID:9684783</ref> <ref>PMID:10233432</ref> <ref>PMID:11588040</ref> <ref>PMID:11897046</ref> <ref>PMID:12083483</ref> <ref>PMID:12353082</ref> <ref>PMID:15583747</ref> <ref>PMID:15634267</ref> <ref>PMID:15748237</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface. [[http://www.uniprot.org/uniprot/ITB3_HUMAN ITB3_HUMAN]] Integrin alpha-V/beta-3 is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.
		+	== 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/vd/2vdp_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 ==
		+	Hemostasis and thrombosis (blood clotting) involve fibrinogen binding to integrin alpha(IIb)beta(3) on platelets, resulting in platelet aggregation. alpha(v)beta(3) binds fibrinogen via an Arg-Asp-Gly (RGD) motif in fibrinogen's alpha subunit. alpha(IIb)beta(3) also binds to fibrinogen; however, it does so via an unstructured RGD-lacking C-terminal region of the gamma subunit (gammaC peptide). These distinct modes of fibrinogen binding enable alpha(IIb)beta(3) and alpha(v)beta(3) to function cooperatively in hemostasis. In this study, crystal structures reveal the integrin alpha(IIb)beta(3)-gammaC peptide interface, and, for comparison, integrin alpha(IIb)beta(3) bound to a lamprey gammaC primordial RGD motif. Compared with RGD, the GAKQAGDV motif in gammaC adopts a different backbone configuration and binds over a more extended region. The integrin metal ion-dependent adhesion site (MIDAS) Mg(2+) ion binds the gammaC Asp side chain. The adjacent to MIDAS (ADMIDAS) Ca(2+) ion binds the gammaC C terminus, revealing a contribution for ADMIDAS in ligand binding. Structural data from this natively disordered gammaC peptide enhances our understanding of the involvement of gammaC peptide and integrin alpha(IIb)beta(3) in hemostasis and thrombosis.

-	~~==Disease==~~	+	Structural basis for distinctive recognition of fibrinogen gammaC peptide by the platelet integrin alphaIIbbeta3.,Springer TA, Zhu J, Xiao T J Cell Biol. 2008 Aug 25;182(4):791-800. Epub 2008 Aug 18. PMID:18710925<ref>PMID:18710925</ref>
-	~~[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Defects in ITGA2B are a cause~~ of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by ~~mucocutaneous bleeding of mild-to-moderate severity and~~ the ~~inability of this~~ integrin ~~to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II~~. ~~In type I~~, ~~platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II~~, ~~the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls)~~, ~~have detectable amounts of fibrinogen, and have low or moderate clot retraction capability~~. ~~The platelets of GT 'variants' have normal or near normal~~ (~~60-100%~~) ~~expression of dysfunctional receptors.<ref>PMID~~:8282784</ref><ref>PMID:7508443</ref><ref>PMID:7706461</ref><ref>PMID:8704171</ref><ref>PMID:9215749</ref><ref>PMID:9473221</ref><ref>PMID:9763559</ref><ref>PMID:9722314</ref><ref>PMID:9734640</ref><ref>PMID:9920835</ref><ref>PMID:10607701</ref><ref>PMID:11798398</ref><ref>PMID:12181054</ref><ref>PMID:12083483</ref><ref>PMID:12424194</ref><ref>PMID:12506038</ref><ref>PMID:15099289</ref><ref>PMID:15219201</ref><ref>PMID:17018384</ref> [[http://www.uniprot.org/uniprot/ITB3_HUMAN ITB3_HUMAN]] Defects in ITGB3 are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-~~to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands~~. ~~GT has been classified clinically into types I and II~~. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:2392682</ref><ref>PMID:1371279</ref><ref>PMID:1602006</ref><ref>PMID:1438206</ref><ref>PMID:8781422</ref><ref>PMID:9376589</ref><ref>PMID:9215749</ref><ref>PMID:9790984</ref><ref>PMID:9684783</ref><ref>PMID:10233432</ref><ref>PMID:11588040</ref><ref>PMID:11897046</ref><ref>PMID:12083483</ref><ref>PMID:12353082</ref><ref>PMID:15583747</ref><ref>PMID:15634267</ref><ref>PMID:~~15748237~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Integrin alpha-IIb/beta-3 is a receptor for fibronectin~~, ~~fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in~~ a ~~wide array~~ of ~~ligands. It recognizes~~ the ~~sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain~~. ~~Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen~~. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface. [[http://www.uniprot.org/uniprot/ITB3_HUMAN ITB3_HUMAN]] Integrin alpha-V/beta-3 is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[2vdp]] is a 5 chain structure with sequence from [http:~~//en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=2VDP OCA].	+

	==See Also==		==See Also==
	*[[Fibrinogen\|Fibrinogen]]		*[[Fibrinogen\|Fibrinogen]]
	*[[Integrin\|Integrin]]		*[[Integrin\|Integrin]]
-		+	*[[Monoclonal Antibody\|Monoclonal Antibody]]
-	==~~Reference~~==	+	== References ==
-	~~<ref group="xtra">PMID:018710925</ref><ref group="xtra">PMID:015378069</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]

OCA at 21:47, 24 March 2013

OCA — Sun, 24 Mar 2013 21:47:53 GMT

←Older revision		Revision as of 21:47, 24 March 2013
Line 1:		Line 1:
-	[[Image:2vdp.png\|left\|200px]]
-
	{{STRUCTURE_2vdp\| PDB=2vdp \| SCENE= }}		{{STRUCTURE_2vdp\| PDB=2vdp \| SCENE= }}
-
	===INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV===		===INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV===
		+	{{ABSTRACT_PUBMED_18710925}}

-	~~{{ABSTRACT_PUBMED_18710925}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Defects in ITGA2B are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:8282784</ref><ref>PMID:7508443</ref><ref>PMID:7706461</ref><ref>PMID:8704171</ref><ref>PMID:9215749</ref><ref>PMID:9473221</ref><ref>PMID:9763559</ref><ref>PMID:9722314</ref><ref>PMID:9734640</ref><ref>PMID:9920835</ref><ref>PMID:10607701</ref><ref>PMID:11798398</ref><ref>PMID:12181054</ref><ref>PMID:12083483</ref><ref>PMID:12424194</ref><ref>PMID:12506038</ref><ref>PMID:15099289</ref><ref>PMID:15219201</ref><ref>PMID:17018384</ref> [[http://www.uniprot.org/uniprot/ITB3_HUMAN ITB3_HUMAN]] Defects in ITGB3 are a cause of Glanzmann thrombasthenia (GT) [MIM:[http://omim.org/entry/273800 273800]]; also known as thrombasthenia of Glanzmann and Naegeli. GT is the most common inherited disease of platelets. It is an autosomal recessive disorder characterized by mucocutaneous bleeding of mild-to-moderate severity and the inability of this integrin to recognize macromolecular or synthetic peptide ligands. GT has been classified clinically into types I and II. In type I, platelets show absence of the glycoprotein IIb/beta-3 complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express the glycoprotein IIb/beta-3 complex at reduced levels (5-20% controls), have detectable amounts of fibrinogen, and have low or moderate clot retraction capability. The platelets of GT 'variants' have normal or near normal (60-100%) expression of dysfunctional receptors.<ref>PMID:2392682</ref><ref>PMID:1371279</ref><ref>PMID:1602006</ref><ref>PMID:1438206</ref><ref>PMID:8781422</ref><ref>PMID:9376589</ref><ref>PMID:9215749</ref><ref>PMID:9790984</ref><ref>PMID:9684783</ref><ref>PMID:10233432</ref><ref>PMID:11588040</ref><ref>PMID:11897046</ref><ref>PMID:12083483</ref><ref>PMID:12353082</ref><ref>PMID:15583747</ref><ref>PMID:15634267</ref><ref>PMID:15748237</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/ITA2B_HUMAN ITA2B_HUMAN]] Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface. [[http://www.uniprot.org/uniprot/ITB3_HUMAN ITB3_HUMAN]] Integrin alpha-V/beta-3 is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.

	==About this Structure==		==About this Structure==
Line 15:		Line 17:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:018710925</ref><ref group="xtra">PMID:015378069</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018710925</ref><ref group="xtra">PMID:015378069</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]

OCA at 07:13, 20 October 2012

OCA — Sat, 20 Oct 2012 07:13:32 GMT

←Older revision		Revision as of 07:13, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[2vdp]] is a 5 chain structure ~~of [[Fibrinogen]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=2VDP OCA].	+	[[2vdp]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=2VDP OCA].

	==See Also==		==See Also==
	*[[Fibrinogen\|Fibrinogen]]		*[[Fibrinogen\|Fibrinogen]]
		+	*[[Integrin\|Integrin]]

	==Reference==		==Reference==

OCA at 15:38, 25 July 2012

OCA — Wed, 25 Jul 2012 15:38:42 GMT

←Older revision		Revision as of 15:38, 25 July 2012
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	[[Image:2vdp.png\|left\|200px]]		[[Image:2vdp.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2vdp", 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_2vdp\| PDB=2vdp \| SCENE= }}		{{STRUCTURE_2vdp\| PDB=2vdp \| SCENE= }}

	===INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV===		===INTEGRIN ALPHAIIBBETA3 HEADPIECE BOUND TO FIBRINOGEN GAMMA CHAIN PEPTIDE,LGGAKQAGDV===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18710925}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18710925 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18710925}}		{{ABSTRACT_PUBMED_18710925}}

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	==See Also==		==See Also==
-	*[[Fibrinogen]]	+	*[[Fibrinogen\|Fibrinogen]]

	==Reference==		==Reference==

OCA at 05:17, 24 August 2011

OCA — Wed, 24 Aug 2011 05:17:27 GMT

←Older revision		Revision as of 05:17, 24 August 2011
Line 25:		Line 25:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18710925~~</ref><ref group="xtra">PMID:~~15378069~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018710925</ref><ref group="xtra">PMID:015378069</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
Line 31:		Line 31:
	[[Category: Xiao, T.]]		[[Category: Xiao, T.]]
	[[Category: Zhu, J.]]		[[Category: Zhu, J.]]
-	[[Category: Alternative splicing]]
	[[Category: Antagonist]]		[[Category: Antagonist]]
-	[[Category: Calcium]]
	[[Category: Cell adhesion]]		[[Category: Cell adhesion]]
-	[[Category: Cell adhesion~~/immune system]]~~	+	[[Category: Cell adhesion-immune system complex]]
-	~~[[Category: Cell adhesion/~~immune system complex]]	+
	[[Category: Cleavage on pair of basic residue]]		[[Category: Cleavage on pair of basic residue]]
	[[Category: Disease mutation]]		[[Category: Disease mutation]]
Line 46:		Line 43:
	[[Category: Phosphorylation]]		[[Category: Phosphorylation]]
	[[Category: Platelet integrin alphaiibbeta3]]		[[Category: Platelet integrin alphaiibbeta3]]
-	[[Category: Polymorphism]]
	[[Category: Pyrrolidone carboxylic acid]]		[[Category: Pyrrolidone carboxylic acid]]
	[[Category: Receptor]]		[[Category: Receptor]]
	[[Category: Transmembrane]]		[[Category: Transmembrane]]

OCA: Protected "2vdp" [edit=sysop:move=sysop]

OCA — Mon, 14 Mar 2011 23:23:59 GMT

Protected "2vdp" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:23, 14 March 2011