1aol - Revision history

OCA at 15:26, 13 March 2024

OCA — Wed, 13 Mar 2024 15:26:33 GMT

←Older revision		Revision as of 15:26, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='1aol' size='340' side='right'caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1aol' size='340' side='right'caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~F-mulv F-mulv~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Friend_murine_leukemia_virus Friend murine leukemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOL FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [https://pdbe.org/1aol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [https://www.ebi.ac.uk/pdbsum/1aol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aol 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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [https://pdbe.org/1aol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [https://www.ebi.ac.uk/pdbsum/1aol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aol ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ENV_MLVF5 ENV_MLVF5]] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).	+	[https://www.uniprot.org/uniprot/ENV_MLVF5 ENV_MLVF5] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 19:		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=1aol 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=1aol ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	An essential step in retrovirus infection is the binding of the virus to its receptor on a target cell. The structure of the receptor-binding domain of the envelope glycoprotein from Friend murine leukemia virus was determined to 2.0 angstrom resolution by x-ray crystallography. The core of the domain is an antiparallel beta sandwich, with two interstrand loops forming a helical subdomain atop the sandwich. The residues in the helical region, but not in the beta sandwich, are highly variable among mammalian C-type retroviruses with distinct tropisms, indicating that the helical subdomain determines the receptor specificity of the virus.
-
-	Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution.,Fass D, Davey RA, Hamson CA, Kim PS, Cunningham JM, Berger JM Science. 1997 Sep 12;277(5332):1662-6. PMID:9287219<ref>PMID:9287219</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1aol" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~F-mulv~~]]	+	[[Category: Friend murine leukemia virus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Berger~~, J M~~]]	+	[[Category: Berger JM]]
-	[[Category: Cunningham~~, J M~~]]	+	[[Category: Cunningham JM]]
-	[[Category: Davey~~, R A~~]]	+	[[Category: Davey RA]]
-	[[Category: Fass, D]]	+	[[Category: Fass D]]
-	[[Category: Hamson~~, C A~~]]	+	[[Category: Hamson CA]]
-	[[Category: Kim~~, P S]]~~	+	[[Category: Kim PS]]
-	~~[[Category: Coat protein]]~~	+
-	~~[[Category: Retrovirus]]~~	+
-	~~[[Category: Viral glycoprotein]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 09:47, 26 May 2021

OCA — Wed, 26 May 2021 09:47:30 GMT

←Older revision		Revision as of 09:47, 26 May 2021
Line 3:		Line 3:
	<StructureSection load='1aol' size='340' side='right'caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1aol' size='340' side='right'caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/F-mulv F-mulv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1AOL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/F-mulv F-mulv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOL FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [~~http~~://pdbe.org/1aol PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1aol PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1aol 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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [https://pdbe.org/1aol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [https://www.ebi.ac.uk/pdbsum/1aol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aol ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ENV_MLVF5 ENV_MLVF5]] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).	+	[[https://www.uniprot.org/uniprot/ENV_MLVF5 ENV_MLVF5]] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:28, 21 August 2019

OCA — Wed, 21 Aug 2019 07:28:05 GMT

←Older revision		Revision as of 07:28, 21 August 2019
Line 1:		Line 1:

	==FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN==		==FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN==
-	<StructureSection load='1aol' size='340' side='right' caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='1aol' size='340' side='right'caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/F-mulv F-mulv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOL FirstGlance]. <br>		<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/F-mulv F-mulv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOL FirstGlance]. <br>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ao/1aol_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ao/1aol_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 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: F-mulv]]		[[Category: F-mulv]]
		+	[[Category: Large Structures]]
	[[Category: Berger, J M]]		[[Category: Berger, J M]]
	[[Category: Cunningham, J M]]		[[Category: Cunningham, J M]]

OCA at 10:49, 15 November 2017

OCA — Wed, 15 Nov 2017 10:49:56 GMT

←Older revision		Revision as of 10:49, 15 November 2017
Line 1:		Line 1:
		+
	==FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN==		==FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN==
	<StructureSection load='1aol' size='340' side='right' caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1aol' size='340' side='right' caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/F-mulv F-mulv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOL FirstGlance]. <br>		<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/F-mulv F-mulv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOL FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [http://pdbe.org/1aol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [http://www.ebi.ac.uk/pdbsum/1aol 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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [http://pdbe.org/1aol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [http://www.ebi.ac.uk/pdbsum/1aol PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aol ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 04:23, 8 February 2016

OCA — Mon, 08 Feb 2016 04:23:42 GMT

←Older revision		Revision as of 04:23, 8 February 2016
Line 16:		Line 16:
	<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=1aol ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 07:49, 10 September 2015

OCA — Thu, 10 Sep 2015 07:49:30 GMT

←Older revision		Revision as of 07:49, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1aol' size='340' side='right' caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1aol' size='340' side='right' caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Friend_murine_leukemia_virus Friend murine leukemia virus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/F-mulv F-mulv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOL FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [http://www.ebi.ac.uk/pdbsum/1aol 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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [http://pdbe.org/1aol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [http://www.ebi.ac.uk/pdbsum/1aol PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 26:		Line 26:
	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 1aol" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Friend murine leukemia virus~~]]	+	[[Category: F-mulv]]
	[[Category: Berger, J M]]		[[Category: Berger, J M]]
	[[Category: Cunningham, J M]]		[[Category: Cunningham, J M]]

OCA at 20:35, 24 December 2014

OCA — Wed, 24 Dec 2014 20:35:39 GMT

←Older revision		Revision as of 20:35, 24 December 2014
Line 6:		Line 6:
	<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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [http://www.ebi.ac.uk/pdbsum/1aol 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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [http://www.ebi.ac.uk/pdbsum/1aol PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ENV_MLVF5 ENV_MLVF5]] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:56, 22 December 2014

OCA — Mon, 22 Dec 2014 09:56:47 GMT

←Older revision		Revision as of 09:56, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Friend_murine_leukemia_virus Friend murine leukemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOL FirstGlance]. <br>		<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Friend_murine_leukemia_virus Friend murine leukemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOL FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [http://www.ebi.ac.uk/pdbsum/1aol 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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [http://www.ebi.ac.uk/pdbsum/1aol PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Friend murine leukemia virus]]		[[Category: Friend murine leukemia virus]]
-	[[Category: Berger, J M.]]	+	[[Category: Berger, J M]]
-	[[Category: Cunningham, J M.]]	+	[[Category: Cunningham, J M]]
-	[[Category: Davey, R A.]]	+	[[Category: Davey, R A]]
-	[[Category: Fass, D.]]	+	[[Category: Fass, D]]
-	[[Category: Hamson, C A.]]	+	[[Category: Hamson, C A]]
-	[[Category: Kim, P S.]]	+	[[Category: Kim, P S]]
	[[Category: Coat protein]]		[[Category: Coat protein]]
	[[Category: Retrovirus]]		[[Category: Retrovirus]]
	[[Category: Viral glycoprotein]]		[[Category: Viral glycoprotein]]
	[[Category: Viral protein]]		[[Category: Viral protein]]

OCA at 08:17, 30 July 2014

OCA — Wed, 30 Jul 2014 08:17:44 GMT

←Older revision		Revision as of 08:17, 30 July 2014
Line 1:		Line 1:
-	[[~~Image~~:1aol.~~png\|left~~\|200px]]	+	==FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN==
		+	<StructureSection load='1aol' size='340' side='right' caption='[[1aol]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1aol]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Friend_murine_leukemia_virus Friend murine leukemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOL FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<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=1aol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aol OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1aol RCSB], [http://www.ebi.ac.uk/pdbsum/1aol 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/ao/1aol_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 ==
		+	An essential step in retrovirus infection is the binding of the virus to its receptor on a target cell. The structure of the receptor-binding domain of the envelope glycoprotein from Friend murine leukemia virus was determined to 2.0 angstrom resolution by x-ray crystallography. The core of the domain is an antiparallel beta sandwich, with two interstrand loops forming a helical subdomain atop the sandwich. The residues in the helical region, but not in the beta sandwich, are highly variable among mammalian C-type retroviruses with distinct tropisms, indicating that the helical subdomain determines the receptor specificity of the virus.

-	~~{{STRUCTURE_1aol\| PDB=1aol \| SCENE= }}~~	+	Structure of a murine leukemia virus receptor-binding glycoprotein at 2.0 angstrom resolution.,Fass D, Davey RA, Hamson CA, Kim PS, Cunningham JM, Berger JM Science. 1997 Sep 12;277(5332):1662-6. PMID:9287219<ref>PMID:9287219</ref>

-	~~===FRIEND MURINE LEUKEMIA VIRUS RECEPTOR-BINDING DOMAIN===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_9287219}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1aol]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Friend_murine_leukemia_virus Friend murine leukemia virus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1AOL OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:009287219<~~/~~ref~~><~~ref group="xtra">PMID:011880627</ref><references group="xtra"~~/>	+
	[[Category: Friend murine leukemia virus]]		[[Category: Friend murine leukemia virus]]
	[[Category: Berger, J M.]]		[[Category: Berger, J M.]]

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

OCA — Sun, 21 Oct 2012 12:26:21 GMT

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

←Older revision

Revision as of 12:26, 21 October 2012