2efl - Revision history

OCA at 08:39, 25 October 2023

OCA — Wed, 25 Oct 2023 08:39:20 GMT

←Older revision		Revision as of 08:39, 25 October 2023
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	<StructureSection load='2efl' size='340' side='right'caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>		<StructureSection load='2efl' size='340' side='right'caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EFL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EFL FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non~~-~~Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.61Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [https://pdbe.org/2efl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [https://www.ebi.ac.uk/pdbsum/2efl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2efl ProSAT], [https://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [https://pdbe.org/2efl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [https://www.ebi.ac.uk/pdbsum/2efl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2efl ProSAT], [https://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.	+	[https://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:15252009</ref> <ref>PMID:16326391</ref> <ref>PMID:16318909</ref> <ref>PMID:16418535</ref> <ref>PMID:17512409</ref>	+	[https://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN] May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:15252009</ref> <ref>PMID:16326391</ref> <ref>PMID:16318909</ref> <ref>PMID:16418535</ref> <ref>PMID:17512409</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Niwa, H]]	+	[[Category: Niwa H]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Shimada A]]
-	[[Category: Shimada, A]]	+	[[Category: Shirouzu M]]
-	[[Category: Shirouzu, M]]	+	[[Category: Terada T]]
-	[[Category: Terada, T]]	+	[[Category: Yokoyama S]]
-	[[Category: Yokoyama, S]]	+
-	~~[[Category: Efc domain]]~~	+
-	~~[[Category: Endocytosis-exocytosis complex]]~~	+
-	~~[[Category: National project on protein structural and functional analyse]]~~	+
-	~~[[Category: Nppsfa]]~~	+
-	~~[[Category: Rsgi~~]]	+

OCA at 17:23, 15 December 2021

OCA — Wed, 15 Dec 2021 17:23:56 GMT

←Older revision		Revision as of 17:23, 15 December 2021
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	<StructureSection load='2efl' size='340' side='right'caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>		<StructureSection load='2efl' size='340' side='right'caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2EFL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EFL FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [~~http~~://pdbe.org/2efl PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2efl PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2efl ProSAT], [~~http~~://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [https://pdbe.org/2efl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [https://www.ebi.ac.uk/pdbsum/2efl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2efl ProSAT], [https://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.	+	[[https://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:15252009</ref> <ref>PMID:16326391</ref> <ref>PMID:16318909</ref> <ref>PMID:16418535</ref> <ref>PMID:17512409</ref>	+	[[https://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:15252009</ref> <ref>PMID:16326391</ref> <ref>PMID:16318909</ref> <ref>PMID:16418535</ref> <ref>PMID:17512409</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:32, 11 March 2020

OCA — Wed, 11 Mar 2020 08:32:17 GMT

←Older revision		Revision as of 08:32, 11 March 2020
Line 1:		Line 1:

	==Crystal structure of the EFC domain of formin-binding protein 17==		==Crystal structure of the EFC domain of formin-binding protein 17==
-	<StructureSection load='2efl' size='340' side='right' caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>	+	<StructureSection load='2efl' size='340' side='right'caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFL FirstGlance]. <br>		<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFL FirstGlance]. <br>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Niwa, H]]		[[Category: Niwa, H]]
	[[Category: Structural genomic]]		[[Category: Structural genomic]]

OCA at 06:45, 6 June 2018

OCA — Wed, 06 Jun 2018 06:45:17 GMT

←Older revision		Revision as of 06:45, 6 June 2018
Line 1:		Line 1:
		+
	==Crystal structure of the EFC domain of formin-binding protein 17==		==Crystal structure of the EFC domain of formin-binding protein 17==
	<StructureSection load='2efl' size='340' side='right' caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>		<StructureSection load='2efl' size='340' side='right' caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFL FirstGlance]. <br>		<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFL FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [http://pdbe.org/2efl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [http://www.ebi.ac.uk/pdbsum/2efl PDBsum], [http://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [http://pdbe.org/2efl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [http://www.ebi.ac.uk/pdbsum/2efl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2efl ProSAT], [http://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/2efl_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/2efl_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>

OCA at 07:52, 10 February 2016

OCA — Wed, 10 Feb 2016 07:52:55 GMT

←Older revision		Revision as of 07:52, 10 February 2016
Line 18:		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=2efl ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 06:52, 11 September 2015

OCA — Fri, 11 Sep 2015 06:52:28 GMT

←Older revision		Revision as of 06:52, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2efl' size='340' side='right' caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>		<StructureSection load='2efl' size='340' side='right' caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFL FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [http://www.ebi.ac.uk/pdbsum/2efl PDBsum], [http://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [http://pdbe.org/2efl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [http://www.ebi.ac.uk/pdbsum/2efl PDBsum], [http://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 28:		Line 28:
	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 2efl" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Niwa, H]]		[[Category: Niwa, H]]
	[[Category: Structural genomic]]		[[Category: Structural genomic]]

OCA at 17:48, 15 January 2015

OCA — Thu, 15 Jan 2015 17:48:30 GMT

←Older revision		Revision as of 17:48, 15 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFL FirstGlance]. <br>		<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFL FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [http://www.ebi.ac.uk/pdbsum/2efl PDBsum], [http://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [http://www.ebi.ac.uk/pdbsum/2efl PDBsum], [http://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.		[[http://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.
Line 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Niwa, H.]]	+	[[Category: Niwa, H]]
-	[[Category: ~~RSGI, RIKEN~~ Structural ~~Genomics/Proteomics Initiative.~~]]	+	[[Category: Structural genomic]]
-	[[Category: Shimada, A.]]	+	[[Category: Shimada, A]]
-	[[Category: Shirouzu, M.]]	+	[[Category: Shirouzu, M]]
-	[[Category: Terada, T.]]	+	[[Category: Terada, T]]
-	[[Category: Yokoyama, S.]]	+	[[Category: Yokoyama, S]]
	[[Category: Efc domain]]		[[Category: Efc domain]]
	[[Category: Endocytosis-exocytosis complex]]		[[Category: Endocytosis-exocytosis complex]]
	[[Category: National project on protein structural and functional analyse]]		[[Category: National project on protein structural and functional analyse]]
	[[Category: Nppsfa]]		[[Category: Nppsfa]]
-	[[Category: Riken structural genomics/proteomics initiative]]
	[[Category: Rsgi]]		[[Category: Rsgi]]
-	[[Category: Structural genomic]]

OCA at 02:35, 30 September 2014

OCA — Tue, 30 Sep 2014 02:35:02 GMT

←Older revision		Revision as of 02:35, 30 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2efl\| PDB=2efl \| SCENE= }}~~	+	==Crystal structure of the EFC domain of formin-binding protein 17==
-	===Crystal structure of the EFC domain of formin-binding protein 17===	+	<StructureSection load='2efl' size='340' side='right' caption='[[2efl]], [[Resolution\|resolution]] 2.61Å' scene=''>
-	~~{{ABSTRACT_PUBMED_17512409}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[2efl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EFL FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2efl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2efl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2efl RCSB], [http://www.ebi.ac.uk/pdbsum/2efl PDBsum], [http://www.topsan.org/Proteins/RSGI/2efl TOPSAN]</span></td></tr>
		+	<table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.		[[http://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:15252009</ref> <ref>PMID:16326391</ref> <ref>PMID:16318909</ref> <ref>PMID:16418535</ref> <ref>PMID:17512409</ref>
		+	== 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/ef/2efl_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 ==
		+	Pombe Cdc15 homology (PCH) proteins play an important role in a variety of actin-based processes, including clathrin-mediated endocytosis (CME). The defining feature of the PCH proteins is an evolutionarily conserved EFC/F-BAR domain for membrane association and tubulation. In the present study, we solved the crystal structures of the EFC domains of human FBP17 and CIP4. The structures revealed a gently curved helical-bundle dimer of approximately 220 A in length, which forms filaments through end-to-end interactions in the crystals. The curved EFC dimer fits a tubular membrane with an approximately 600 A diameter. We subsequently proposed a model in which the curved EFC filament drives tubulation. In fact, striation of tubular membranes was observed by phase-contrast cryo-transmission electron microscopy, and mutations that impaired filament formation also impaired membrane tubulation and cell membrane invagination. Furthermore, FBP17 is recruited to clathrin-coated pits in the late stage of CME, indicating its physiological role.

-	~~==Function==~~	+	Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis.,Shimada A, Niwa H, Tsujita K, Suetsugu S, Nitta K, Hanawa-Suetsugu K, Akasaka R, Nishino Y, Toyama M, Chen L, Liu ZJ, Wang BC, Yamamoto M, Terada T, Miyazawa A, Tanaka A, Sugano S, Shirouzu M, Nagayama K, Takenawa T, Yokoyama S Cell. 2007 May 18;129(4):761-72. PMID:17512409<ref>PMID:17512409</ref>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] May act as~~ a ~~link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate~~ membrane ~~tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated~~ endocytosis. ~~Binds to lipids such as phosphatidylinositol 4~~,5-~~bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP~~, ~~which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles~~. May ~~be required for the lysosomal retention of FASLG/FASL~~.~~<ref>~~PMID:~~15252009</ref><ref>PMID:16326391</ref><ref>PMID:16318909</ref><ref>PMID:16418535</ref>~~<ref>PMID:17512409</ref>	+
-		+
-	~~==About this Structure==~~	+
-	[[2efl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EFL OCA].	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:017512409</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Niwa, H.]]		[[Category: Niwa, H.]]

OCA at 02:21, 25 March 2013

OCA — Mon, 25 Mar 2013 02:21:30 GMT

←Older revision		Revision as of 02:21, 25 March 2013
Line 1:		Line 1:
-	[[Image:2efl.png\|left\|200px]]
-
	{{STRUCTURE_2efl\| PDB=2efl \| SCENE= }}		{{STRUCTURE_2efl\| PDB=2efl \| SCENE= }}
-
	===Crystal structure of the EFC domain of formin-binding protein 17===		===Crystal structure of the EFC domain of formin-binding protein 17===
		+	{{ABSTRACT_PUBMED_17512409}}

-	~~{{ABSTRACT_PUBMED_17512409}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with MLL. The relatively low incidence of the MLL-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/FNBP1_HUMAN FNBP1_HUMAN]] May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.<ref>PMID:15252009</ref><ref>PMID:16326391</ref><ref>PMID:16318909</ref><ref>PMID:16418535</ref><ref>PMID:17512409</ref>

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:017512409</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017512409</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Niwa, H.]]		[[Category: Niwa, H.]]

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

OCA — Sun, 06 Jan 2013 11:47:26 GMT

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

←Older revision

Revision as of 11:47, 6 January 2013