1cjf - Revision history

OCA at 05:52, 9 August 2023

2023-08-09T05:52:53Z

←Older revision		Revision as of 05:52, 9 August 2023
Line 3:		Line 3:
	<StructureSection load='1cjf' size='340' side='right'caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1cjf' size='340' side='right'caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJF FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</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]] 2.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [https://pdbe.org/1cjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [https://www.ebi.ac.uk/pdbsum/1cjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjf 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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [https://pdbe.org/1cjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [https://www.ebi.ac.uk/pdbsum/1cjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjf ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18) [MIM:[https://omim.org/entry/614808 614808]]. A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.<ref>PMID:22801503</ref>	+	[https://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN] Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18) [MIM:[https://omim.org/entry/614808 614808]. A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.<ref>PMID:22801503</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.<ref>PMID:18573880</ref>	+	[https://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.<ref>PMID:18573880</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Almo~~, S C~~]]	+	[[Category: Almo SC]]
-	[[Category: Fedorov~~, A A~~]]	+	[[Category: Fedorov AA]]
-	[[Category: Fedorov, E]]	+	[[Category: Fedorov E]]
-	[[Category: Mahoney~~, N M~~]]	+	[[Category: Mahoney NM]]
-	[[Category: Rozwarski~~, D A]]~~	+	[[Category: Rozwarski DA]]
-	~~[[Category: Actin-binding protein]]~~	+
-	~~[[Category: Cytoskeleton]]~~	+
-	~~[[Category: Poly-l-proline]]~~	+
-	~~[[Category: Profilin]]~~	+
-	~~[[Category: Structural regulation protein~~]]	+

OCA at 10:43, 19 May 2021

2021-05-19T10:43:45Z

←Older revision		Revision as of 10:43, 19 May 2021
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	<StructureSection load='1cjf' size='340' side='right'caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1cjf' size='340' side='right'caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1CJF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJF FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [~~http~~://pdbe.org/1cjf PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1cjf PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjf 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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [https://pdbe.org/1cjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [https://www.ebi.ac.uk/pdbsum/1cjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjf ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18) [MIM:[~~http~~://omim.org/entry/614808 614808]]. A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.<ref>PMID:22801503</ref>	+	[[https://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18) [MIM:[https://omim.org/entry/614808 614808]]. A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.<ref>PMID:22801503</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.<ref>PMID:18573880</ref>	+	[[https://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.<ref>PMID:18573880</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:

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

OCA at 18:02, 14 August 2019

2019-08-14T18:02:11Z

←Older revision		Revision as of 18:02, 14 August 2019
Line 1:		Line 1:

	==PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS==		==PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS==
-	<StructureSection load='1cjf' size='340' side='right' caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='1cjf' size='340' side='right'caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJF FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJF FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/1cjf_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/1cjf_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 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1cjf" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1cjf" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Profilin\|Profilin]]
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Almo, S C]]		[[Category: Almo, S C]]
	[[Category: Fedorov, A A]]		[[Category: Fedorov, A A]]

OCA at 10:42, 8 November 2017

2017-11-08T10:42:31Z

←Older revision		Revision as of 10:42, 8 November 2017
Line 1:		Line 1:
		+
	==PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS==		==PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS==
	<StructureSection load='1cjf' size='340' side='right' caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1cjf' size='340' side='right' caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJF FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [http://pdbe.org/1cjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [http://www.ebi.ac.uk/pdbsum/1cjf 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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [http://pdbe.org/1cjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [http://www.ebi.ac.uk/pdbsum/1cjf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjf ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1cjf" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1cjf" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Profilin\|Profilin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:12, 7 February 2016

2016-02-07T11:12:10Z

←Older revision		Revision as of 11:12, 7 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=1cjf ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 00:56, 10 September 2015

2015-09-10T00:56:39Z

←Older revision		Revision as of 00:56, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1cjf' size='340' side='right' caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1cjf' size='340' side='right' caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [http://www.ebi.ac.uk/pdbsum/1cjf 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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [http://pdbe.org/1cjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [http://www.ebi.ac.uk/pdbsum/1cjf PDBsum]</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 1cjf" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Profilin\|Profilin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Almo, S C]]		[[Category: Almo, S C]]
	[[Category: Fedorov, A A]]		[[Category: Fedorov, A A]]

OCA at 22:08, 22 December 2014

2014-12-22T22:08:43Z

←Older revision		Revision as of 22:08, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJF FirstGlance]. <br>		<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJF FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [http://www.ebi.ac.uk/pdbsum/1cjf 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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [http://www.ebi.ac.uk/pdbsum/1cjf PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18) [MIM:[http://omim.org/entry/614808 614808]]. A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.<ref>PMID:22801503</ref>		[[http://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18) [MIM:[http://omim.org/entry/614808 614808]]. A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.<ref>PMID:22801503</ref>
Line 33:		Line 33:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Almo, S C.]]	+	[[Category: Almo, S C]]
-	[[Category: Fedorov, A A.]]	+	[[Category: Fedorov, A A]]
-	[[Category: Fedorov, E.]]	+	[[Category: Fedorov, E]]
-	[[Category: Mahoney, N M.]]	+	[[Category: Mahoney, N M]]
-	[[Category: Rozwarski, D A.]]	+	[[Category: Rozwarski, D A]]
	[[Category: Actin-binding protein]]		[[Category: Actin-binding protein]]
	[[Category: Cytoskeleton]]		[[Category: Cytoskeleton]]

OCA at 16:03, 29 September 2014

2014-09-29T16:03:45Z

←Older revision		Revision as of 16:03, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1cjf\| PDB=1cjf \| SCENE= }}~~	+	==PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS==
-	===PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS===	+	<StructureSection load='1cjf' size='340' side='right' caption='[[1cjf]], [[Resolution\|resolution]] 2.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_10404225}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1cjf]] is a 4 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=1CJF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJF FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HOM:7-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARIN'>HOM</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=1cjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cjf RCSB], [http://www.ebi.ac.uk/pdbsum/1cjf PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18) [MIM:[http://omim.org/entry/614808 614808]]. A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.<ref>PMID:22801503</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.<ref>PMID:18573880</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/cj/1cjf_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 ==
		+	The actin regulatory protein profilin is targeted to specific cellular regions through interactions with highly proline-rich motifs embedded within its binding partners. New X-ray crystallographic results demonstrate that profilin, like SH3 domains, can bind proline-rich ligands in two distinct amide backbone orientations. By further analogy with SH3 domains, these data suggest that non-proline residues in profilin ligands may dictate the polarity and register of binding, and the detailed organization of the assemblies involving profilin. This degeneracy may be a general feature of modules that bind proline-rich ligands, including WW and EVH1 domains, and has implications for the assembly and activity of macromolecular complexes involved in signaling and the regulation of the actin cytoskeleton.

-	~~==Disease==~~	+	Profilin binds proline-rich ligands in two distinct amide backbone orientations.,Mahoney NM, Rozwarski DA, Fedorov E, Fedorov AA, Almo SC Nat Struct Biol. 1999 Jul;6(7):666-71. PMID:10404225<ref>PMID:10404225</ref>
-	~~[[http://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Defects~~ in ~~PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18) [MIM:[http://omim~~.~~org/entry/614808 614808]]. A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord~~, ~~resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons~~, ~~presence of ubiquitin-positive inclusions within surviving motor neurons~~, ~~and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial~~, ~~involving both genetic and environmental factors~~. ~~The disease is inherited in 5~~-~~10% of the cases~~.<ref>PMID:~~22801503~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Binds to actin and affects the structure~~ of the ~~cytoskeleton~~. ~~At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations~~. ~~By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition~~ of AR.<~~ref~~>~~PMID:18573880~~</~~ref~~>	+	</div>
-		+	== References ==
-	==~~About this Structure==~~	+	<references/>
-	[[1cjf]] is a 4 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=1CJF OCA].	+	__TOC__
-		+	</StructureSection>
-	~~==Reference~~==	+
-	~~<ref group="xtra">PMID:010404225</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Almo, S C.]]		[[Category: Almo, S C.]]

OCA at 18:43, 24 March 2013

2013-03-24T18:43:06Z

←Older revision		Revision as of 18:43, 24 March 2013
Line 1:		Line 1:
-	[[Image:1cjf.png\|left\|200px]]
-
	{{STRUCTURE_1cjf\| PDB=1cjf \| SCENE= }}		{{STRUCTURE_1cjf\| PDB=1cjf \| SCENE= }}
-
	===PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS===		===PROFILIN BINDS PROLINE-RICH LIGANDS IN TWO DISTINCT AMIDE BACKBONE ORIENTATIONS===
		+	{{ABSTRACT_PUBMED_10404225}}

-	~~{{ABSTRACT_PUBMED_10404225}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18) [MIM:[http://omim.org/entry/614808 614808]]. A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.<ref>PMID:22801503</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/PROF1_HUMAN PROF1_HUMAN]] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.<ref>PMID:18573880</ref>

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

	==Reference==		==Reference==
-	<ref group="xtra">PMID:010404225</ref><references group="xtra"/>	+	<ref group="xtra">PMID:010404225</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Almo, S C.]]		[[Category: Almo, S C.]]

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

2012-10-21T20:28:58Z

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

←Older revision

Revision as of 20:28, 21 October 2012