1ky6 - Revision history

OCA at 09:06, 16 August 2023

OCA — Wed, 16 Aug 2023 09:06:38 GMT

←Older revision		Revision as of 09:06, 16 August 2023
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	<StructureSection load='1ky6' size='340' side='right'caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1ky6' size='340' side='right'caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=SO4:SULFATE+ION'>SO4</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='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1qtp\|1qtp]], [[1qts\|1qts]], [[1kyu\|1kyu]], [[1ky7\|1ky7]], [[1kyd\|1kyd]], [[1kyf\|1kyf]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [https://pdbe.org/1ky6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ky6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ky6 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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [https://pdbe.org/1ky6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ky6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ky6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/AP2A2_MOUSE AP2A2_MOUSE]] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif.<ref>PMID:10459011</ref> <ref>PMID:14745134</ref> <ref>PMID:15473838</ref> [[https://www.uniprot.org/uniprot/EPN1_RAT EPN1_RAT]] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.<ref>PMID:9723620</ref> <ref>PMID:11161217</ref> <ref>PMID:12353027</ref>	+	[https://www.uniprot.org/uniprot/AP2A2_MOUSE AP2A2_MOUSE] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif.<ref>PMID:10459011</ref> <ref>PMID:14745134</ref> <ref>PMID:15473838</ref>
	== 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: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: ~~Brett, T J~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Fremont, D H~~]]	+	[[Category: Brett TJ]]
-	[[Category: ~~Traub, L M~~]]	+	[[Category: Fremont DH]]
-	[[Category: ~~Endocytosis]]~~	+	[[Category: Traub LM]]
-	~~[[Category: Endocytosis-exocytosis complex]]~~	+
-	~~[[Category: Protein-peptide complex~~]]	+

OCA at 06:36, 18 August 2021

OCA — Wed, 18 Aug 2021 06:36:58 GMT

←Older revision		Revision as of 06:36, 18 August 2021
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	<StructureSection load='1ky6' size='340' side='right'caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1ky6' size='340' side='right'caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qtp\|1qtp]], [[1qts\|1qts]], [[1kyu\|1kyu]], [[1ky7\|1ky7]], [[1kyd\|1kyd]], [[1kyf\|1kyf]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qtp\|1qtp]], [[1qts\|1qts]], [[1kyu\|1kyu]], [[1ky7\|1ky7]], [[1kyd\|1kyd]], [[1kyf\|1kyf]]</div></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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [~~http~~://pdbe.org/1ky6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1ky6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1ky6 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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [https://pdbe.org/1ky6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ky6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ky6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AP2A2_MOUSE AP2A2_MOUSE]] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif.<ref>PMID:10459011</ref> <ref>PMID:14745134</ref> <ref>PMID:15473838</ref> [[~~http~~://www.uniprot.org/uniprot/EPN1_RAT EPN1_RAT]] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.<ref>PMID:9723620</ref> <ref>PMID:11161217</ref> <ref>PMID:12353027</ref>	+	[[https://www.uniprot.org/uniprot/AP2A2_MOUSE AP2A2_MOUSE]] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif.<ref>PMID:10459011</ref> <ref>PMID:14745134</ref> <ref>PMID:15473838</ref> [[https://www.uniprot.org/uniprot/EPN1_RAT EPN1_RAT]] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.<ref>PMID:9723620</ref> <ref>PMID:11161217</ref> <ref>PMID:12353027</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 12:18, 13 November 2019

OCA — Wed, 13 Nov 2019 12:18:03 GMT

←Older revision		Revision as of 12:18, 13 November 2019
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	==AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE==		==AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE==
-	<StructureSection load='1ky6' size='340' side='right' caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='1ky6' size='340' side='right'caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>
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	</div>		</div>
	<div class="pdbe-citations 1ky6" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ky6" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Adaptin 3D structures\|Adaptin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Brett, T J]]		[[Category: Brett, T J]]

OCA at 21:27, 24 January 2018

OCA — Wed, 24 Jan 2018 21:27:41 GMT

←Older revision		Revision as of 21:27, 24 January 2018
Line 1:		Line 1:
		+
	==AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE==		==AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE==
	<StructureSection load='1ky6' size='340' side='right' caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1ky6' size='340' side='right' caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qtp\|1qtp]], [[1qts\|1qts]], [[1kyu\|1kyu]], [[1ky7\|1ky7]], [[1kyd\|1kyd]], [[1kyf\|1kyf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qtp\|1qtp]], [[1qts\|1qts]], [[1kyu\|1kyu]], [[1ky7\|1ky7]], [[1kyd\|1kyd]], [[1kyf\|1kyf]]</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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [http://pdbe.org/1ky6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ky6 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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [http://pdbe.org/1ky6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ky6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ky6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 13:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ky/1ky6_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ky/1ky6_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 28:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 1ky6" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1ky6" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Adaptin\|Adaptin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:11, 9 February 2016

OCA — Tue, 09 Feb 2016 11:11:50 GMT

←Older revision		Revision as of 11:11, 9 February 2016
Line 17:		Line 17:
	<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=1ky6 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 21:44, 10 September 2015

OCA — Thu, 10 Sep 2015 21:44:30 GMT

←Older revision		Revision as of 21:44, 10 September 2015
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	<StructureSection load='1ky6' size='340' side='right' caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1ky6' size='340' side='right' caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qtp\|1qtp]], [[1qts\|1qts]], [[1kyu\|1kyu]], [[1ky7\|1ky7]], [[1kyd\|1kyd]], [[1kyf\|1kyf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qtp\|1qtp]], [[1qts\|1qts]], [[1kyu\|1kyu]], [[1ky7\|1ky7]], [[1kyd\|1kyd]], [[1kyf\|1kyf]]</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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ky6 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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [http://pdbe.org/1ky6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ky6 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1ky6" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 34:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Brett, T J]]		[[Category: Brett, T J]]
	[[Category: Fremont, D H]]		[[Category: Fremont, D H]]

OCA at 06:30, 25 December 2014

OCA — Thu, 25 Dec 2014 06:30:17 GMT

←Older revision		Revision as of 06:30, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qtp\|1qtp]], [[1qts\|1qts]], [[1kyu\|1kyu]], [[1ky7\|1ky7]], [[1kyd\|1kyd]], [[1kyf\|1kyf]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qtp\|1qtp]], [[1qts\|1qts]], [[1kyu\|1kyu]], [[1ky7\|1ky7]], [[1kyd\|1kyd]], [[1kyf\|1kyf]]</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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ky6 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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ky6 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AP2A2_MOUSE AP2A2_MOUSE]] Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif.<ref>PMID:10459011</ref> <ref>PMID:14745134</ref> <ref>PMID:15473838</ref> [[http://www.uniprot.org/uniprot/EPN1_RAT EPN1_RAT]] Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations. Regulates receptor-mediated endocytosis.<ref>PMID:9723620</ref> <ref>PMID:11161217</ref> <ref>PMID:12353027</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 33:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
-	[[Category: Brett, T J.]]	+	[[Category: Brett, T J]]
-	[[Category: Fremont, D H.]]	+	[[Category: Fremont, D H]]
-	[[Category: Traub, L M.]]	+	[[Category: Traub, L M]]
	[[Category: Endocytosis]]		[[Category: Endocytosis]]
	[[Category: Endocytosis-exocytosis complex]]		[[Category: Endocytosis-exocytosis complex]]
	[[Category: Protein-peptide complex]]		[[Category: Protein-peptide complex]]

OCA at 18:01, 28 September 2014

OCA — Sun, 28 Sep 2014 18:01:44 GMT

←Older revision		Revision as of 18:01, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1ky6.~~png~~\|~~left~~\|200px]]	+	==AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE==
		+	<StructureSection load='1ky6' size='340' side='right' caption='[[1ky6]], [[Resolution\|resolution]] 2.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1ky6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KY6 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qtp\|1qtp]], [[1qts\|1qts]], [[1kyu\|1kyu]], [[1ky7\|1ky7]], [[1kyd\|1kyd]], [[1kyf\|1kyf]]</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=1ky6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ky6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ky6 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/ky/1ky6_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 ==
		+	Clathrin-mediated endocytosis depends upon the interaction of accessory proteins with the alpha-ear of the AP-2 adaptor. We present structural characterization of these regulatory interactions. DPF and DPW motif peptides derived from eps15 and epsin bind in type I beta turn conformations to a conserved pocket on the alpha-ear platform. We show evidence for a second binding site that is DPW motif specific. The structure of a complex with an AP-2 binding segment from amphiphysin reveals a novel binding motif that we term FxDxF, which is engaged in an extended conformation by a unique surface of the platform domain. The FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP. A mechanism of clathrin assembly regulation is suggested by three different AP-2 engagement modes.

-	~~{{STRUCTURE_1ky6\| PDB=1ky6 \| SCENE= }}~~	+	Accessory protein recruitment motifs in clathrin-mediated endocytosis.,Brett TJ, Traub LM, Fremont DH Structure. 2002 Jun;10(6):797-809. PMID:12057195<ref>PMID:12057195</ref>

-	~~===AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_12057195}}~~	+	==See Also==
-		+	*[[Adaptin\|Adaptin]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~1ky6~~]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:012057195<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Brett, T J.]]		[[Category: Brett, T J.]]

OCA: Protected "1ky6" [edit=sysop:move=sysop]

OCA — Wed, 05 Dec 2012 20:55:49 GMT

Protected "1ky6" [edit=sysop:move=sysop]

←Older revision

Revision as of 20:55, 5 December 2012

OCA at 20:55, 5 December 2012

OCA — Wed, 05 Dec 2012 20:55:47 GMT

←Older revision		Revision as of 20:55, 5 December 2012
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-	{{Seed}}
	[[Image:1ky6.png\|left\|200px]]		[[Image:1ky6.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1ky6", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1ky6\| PDB=1ky6 \| SCENE= }}		{{STRUCTURE_1ky6\| PDB=1ky6 \| SCENE= }}

	===AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE===		===AP-2 CLATHRIN ADAPTOR ALPHA-APPENDAGE IN COMPLEX WITH EPSIN DPW PEPTIDE===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12057195}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12057195 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_12057195}}		{{ABSTRACT_PUBMED_12057195}}

	==About this Structure==		==About this Structure==
-	~~1KY6~~ is a 2 ~~chains~~ structure ~~of sequences~~ from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA].	+	[[1ky6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KY6 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12057195~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012057195</ref><references group="xtra"/>
	[[Category: Mus musculus]]		[[Category: Mus musculus]]
	[[Category: Brett, T J.]]		[[Category: Brett, T J.]]
Line 29:		Line 17:
	[[Category: Traub, L M.]]		[[Category: Traub, L M.]]
	[[Category: Endocytosis]]		[[Category: Endocytosis]]
		+	[[Category: Endocytosis-exocytosis complex]]
	[[Category: Protein-peptide complex]]		[[Category: Protein-peptide complex]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 09:24:23 2009''