5a1u - Revision history

OCA at 11:34, 9 May 2024

OCA — Thu, 09 May 2024 11:34:54 GMT

←Older revision		Revision as of 11:34, 9 May 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A1U FirstGlance]. <br>		<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A1U FirstGlance]. <br>
-	</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=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [https://pdbe.org/5a1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [https://www.ebi.ac.uk/pdbsum/5a1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1u ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 13Å</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=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [https://pdbe.org/5a1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [https://www.ebi.ac.uk/pdbsum/5a1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 5a1u" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5a1u" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Coatomer 3D structures\|Coatomer 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:52, 18 May 2023

OCA — Thu, 18 May 2023 07:52:38 GMT

←Older revision		Revision as of 07:52, 18 May 2023
Line 3:		Line 3:
	<SX load='5a1u' size='340' side='right' viewer='molstar' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>		<SX load='5a1u' size='340' side='right' viewer='molstar' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_18824 Atcc 18824~~] and [~~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=5A1U OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5A1U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A1U FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5a1v\|5a1v]], [[5a1w\|5a1w]], [[5a1x\|5a1x]], [[5a1y\|5a1y]]</td></tr>~~	+	</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=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [https://pdbe.org/5a1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [https://www.ebi.ac.uk/pdbsum/5a1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1u ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [~~http~~://pdbe.org/5a1u PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5a1u PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1u ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/COPB_MOUSE COPB_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1 (By similarity). Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.<ref>PMID:17698811</ref> <ref>PMID:19067489</ref> [[http://www.uniprot.org/uniprot/COPG1_MOUSE COPG1_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.<ref>PMID:19067489</ref> [[http://www.uniprot.org/uniprot/ARF1_YEAST ARF1_YEAST]] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.<ref>PMID:15356266</ref> [[http://www.uniprot.org/uniprot/COPB2_MOUSE COPB2_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner. [[http://www.uniprot.org/uniprot/COPD_MOUSE COPD_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). [[http://www.uniprot.org/uniprot/COPA_MOUSE COPA_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor (By similarity). [[http://www.uniprot.org/uniprot/COPZ1_MOUSE COPZ1_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.	+	[https://www.uniprot.org/uniprot/ARF1_YEAST ARF1_YEAST] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.<ref>PMID:15356266</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: Atcc 18824]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: ~~Appen, A von~~]]	+	[[Category: Saccharomyces cerevisiae]]
-	[[Category: Beck, M]]	+	[[Category: Beck M]]
-	[[Category: Beck, R]]	+	[[Category: Beck R]]
-	[[Category: Briggs~~, J A.G~~]]	+	[[Category: Briggs JAG]]
-	[[Category: Diestelkoetter-Bachert, P]]	+	[[Category: Diestelkoetter-Bachert P]]
-	[[Category: Dodonova~~, S O~~]]	+	[[Category: Dodonova SO]]
-	[[Category: Hagen~~, W J.H~~]]	+	[[Category: Hagen WJH]]
-	[[Category: Wieland, F]]	+	[[Category: Wieland F]]
-	[[Category: ~~Coated vesicle]]~~	+	[[Category: Von Appen A]]
-	~~[[Category: Coatomer]]~~	+
-	~~[[Category: Copi]]~~	+
-	~~[[Category: Structural protein]]~~	+
-	~~[[Category: Transport protein~~]]	+

OCA at 19:34, 10 April 2020

OCA — Fri, 10 Apr 2020 19:34:27 GMT

←Older revision		Revision as of 19:34, 10 April 2020
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	<SX load='5a1u' size='340' side='right' viewer='molstar' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>		<SX load='5a1u' size='340' side='right' viewer='molstar' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [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=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5A1U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [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=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5A1U FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5a1v\|5a1v]], [[5a1w\|5a1w]], [[5a1x\|5a1x]], [[5a1y\|5a1y]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5a1v\|5a1v]], [[5a1w\|5a1w]], [[5a1x\|5a1x]], [[5a1y\|5a1y]]</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=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [http://pdbe.org/5a1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [http://www.ebi.ac.uk/pdbsum/5a1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1u ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [http://pdbe.org/5a1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [http://www.ebi.ac.uk/pdbsum/5a1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 18:06, 6 March 2020

OCA — Fri, 06 Mar 2020 18:06:45 GMT

←Older revision		Revision as of 18:06, 6 March 2020
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	==The structure of the COPI coat triad==		==The structure of the COPI coat triad==
-	<~~StructureSection~~ load='5a1u' size='340' side='right'caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>	+	<SX load='5a1u' size='340' side='right' viewer='molstar' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [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=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1U FirstGlance]. <br>		<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [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=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1U FirstGlance]. <br>
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	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Atcc 18824]]		[[Category: Atcc 18824]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 07:31, 4 March 2020

OCA — Wed, 04 Mar 2020 07:31:16 GMT

←Older revision		Revision as of 07:31, 4 March 2020
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	==The structure of the COPI coat triad==		==The structure of the COPI coat triad==
-	<StructureSection load='5a1u' size='340' side='right' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>	+	<StructureSection load='5a1u' size='340' side='right'caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [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=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1U FirstGlance]. <br>		<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [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=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1U FirstGlance]. <br>
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 18824]]		[[Category: Atcc 18824]]
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Appen, A von]]		[[Category: Appen, A von]]

OCA at 22:51, 15 November 2017

OCA — Wed, 15 Nov 2017 22:51:31 GMT

←Older revision		Revision as of 22:51, 15 November 2017
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	<StructureSection load='5a1u' size='340' side='right' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>		<StructureSection load='5a1u' size='340' side='right' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1U FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [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=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1U FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5a1v\|5a1v]], [[5a1w\|5a1w]], [[5a1x\|5a1x]], [[5a1y\|5a1y]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5a1v\|5a1v]], [[5a1w\|5a1w]], [[5a1x\|5a1x]], [[5a1y\|5a1y]]</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=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [http://pdbe.org/5a1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [http://www.ebi.ac.uk/pdbsum/5a1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1u ProSAT]</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=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [http://pdbe.org/5a1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [http://www.ebi.ac.uk/pdbsum/5a1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1u ProSAT]</span></td></tr>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 18824]]
		+	[[Category: Lk3 transgenic mice]]
	[[Category: Appen, A von]]		[[Category: Appen, A von]]
	[[Category: Beck, M]]		[[Category: Beck, M]]

OCA at 14:16, 27 April 2017

OCA — Thu, 27 Apr 2017 14:16:38 GMT

←Older revision		Revision as of 14:16, 27 April 2017
Line 1:		Line 1:
		+
	==The structure of the COPI coat triad==		==The structure of the COPI coat triad==
	<StructureSection load='5a1u' size='340' side='right' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>		<StructureSection load='5a1u' size='340' side='right' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1U FirstGlance]. <br>		<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1U FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5a1v\|5a1v]], [[5a1w\|5a1w]], [[5a1x\|5a1x]], [[5a1y\|5a1y]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5a1v\|5a1v]], [[5a1w\|5a1w]], [[5a1x\|5a1x]], [[5a1y\|5a1y]]</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=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [http://www.ebi.ac.uk/pdbsum/5a1u 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=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [http://pdbe.org/5a1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [http://www.ebi.ac.uk/pdbsum/5a1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1u ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 5a1u" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:02, 22 July 2015

OCA — Wed, 22 Jul 2015 08:02:37 GMT

←Older revision		Revision as of 08:02, 22 July 2015
Line 8:		Line 8:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/COPB_MOUSE COPB_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1 (By similarity). Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.<ref>PMID:17698811</ref> <ref>PMID:19067489</ref> [[http://www.uniprot.org/uniprot/COPG1_MOUSE COPG1_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.<ref>PMID:19067489</ref> [[http://www.uniprot.org/uniprot/ARF1_YEAST ARF1_YEAST]] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.<ref>PMID:15356266</ref> [[http://www.uniprot.org/uniprot/COPB2_MOUSE COPB2_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner. [[http://www.uniprot.org/uniprot/COPD_MOUSE COPD_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). [[http://www.uniprot.org/uniprot/COPA_MOUSE COPA_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor (By similarity). [[http://www.uniprot.org/uniprot/COPZ1_MOUSE COPZ1_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.		[[http://www.uniprot.org/uniprot/COPB_MOUSE COPB_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1 (By similarity). Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.<ref>PMID:17698811</ref> <ref>PMID:19067489</ref> [[http://www.uniprot.org/uniprot/COPG1_MOUSE COPG1_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.<ref>PMID:19067489</ref> [[http://www.uniprot.org/uniprot/ARF1_YEAST ARF1_YEAST]] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.<ref>PMID:15356266</ref> [[http://www.uniprot.org/uniprot/COPB2_MOUSE COPB2_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner. [[http://www.uniprot.org/uniprot/COPD_MOUSE COPD_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). [[http://www.uniprot.org/uniprot/COPA_MOUSE COPA_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor (By similarity). [[http://www.uniprot.org/uniprot/COPZ1_MOUSE COPZ1_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Transport of material within cells is mediated by trafficking vesicles that bud from one cellular compartment and fuse with another. Formation of a trafficking vesicle is driven by membrane coats that localize cargo and polymerize into cages to bend the membrane. Although extensive structural information is available for components of these coats, the heterogeneity of trafficking vesicles has prevented an understanding of how complete membrane coats assemble on the membrane. We combined cryo-electron tomography, subtomogram averaging, and cross-linking mass spectrometry to derive a complete model of the assembled coat protein complex I (COPI) coat involved in traffic between the Golgi and the endoplasmic reticulum. The highly interconnected COPI coat structure contradicted the current "adaptor-and-cage" understanding of coated vesicle formation.
		+
		+	VESICULAR TRANSPORT. A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly.,Dodonova SO, Diestelkoetter-Bachert P, von Appen A, Hagen WJ, Beck R, Beck M, Wieland F, Briggs JA Science. 2015 Jul 10;349(6244):195-8. doi: 10.1126/science.aab1121. PMID:26160949<ref>PMID:26160949</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:55, 8 July 2015

OCA — Wed, 08 Jul 2015 14:55:15 GMT

←Older revision		Revision as of 14:55, 8 July 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==The structure of the COPI coat triad==
-		+	<StructureSection load='5a1u' size='340' side='right' caption='[[5a1u]], [[Resolution\|resolution]] 13.00Å' scene=''>
-	~~The entry~~ 5a1u is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5a1u]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A1U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1U FirstGlance]. <br>
-	~~Authors~~: ~~Dodonova~~, S.O., ~~Diestelkoetter~~-~~Bachert~~, P., ~~von Appen~~, A., ~~Hagen~~, W.J.H., ~~Beck~~, R., ~~Beck~~, M., ~~Wieland, F~~., ~~Briggs~~, J.A.G.	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5a1v\|5a1v]], [[5a1w\|5a1w]], [[5a1x\|5a1x]], [[5a1y\|5a1y]]</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=5a1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1u OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5a1u RCSB], [http://www.ebi.ac.uk/pdbsum/5a1u PDBsum]</span></td></tr>
-	~~Description~~: ~~The structure of~~ the COPI ~~coat triad~~	+	</table>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	== Function ==
-	[[~~Category~~: ~~Von Appen, A~~]]	+	[[http://www.uniprot.org/uniprot/COPB_MOUSE COPB_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1 (By similarity). Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.<ref>PMID:17698811</ref> <ref>PMID:19067489</ref> [[http://www.uniprot.org/uniprot/COPG1_MOUSE COPG1_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis.<ref>PMID:19067489</ref> [[http://www.uniprot.org/uniprot/ARF1_YEAST ARF1_YEAST]] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.<ref>PMID:15356266</ref> [[http://www.uniprot.org/uniprot/COPB2_MOUSE COPB2_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner. [[http://www.uniprot.org/uniprot/COPD_MOUSE COPD_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). [[http://www.uniprot.org/uniprot/COPA_MOUSE COPA_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor (By similarity). [[http://www.uniprot.org/uniprot/COPZ1_MOUSE COPZ1_MOUSE]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
-	[[~~Category~~: ~~Beck, R~~]]	+	== References ==
-	[[~~Category~~: ~~Hagen, W~~.J.H]]	+	<references/>
-	[[Category: ~~Briggs~~, J.A.G]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Appen, A von]]
	[[Category: Beck, M]]		[[Category: Beck, M]]
		+	[[Category: Beck, R]]
		+	[[Category: Briggs, J A.G]]
	[[Category: Diestelkoetter-Bachert, P]]		[[Category: Diestelkoetter-Bachert, P]]
		+	[[Category: Dodonova, S O]]
		+	[[Category: Hagen, W J.H]]
	[[Category: Wieland, F]]		[[Category: Wieland, F]]
-	[[Category: ~~Dodonova, S.O~~]]	+	[[Category: Coated vesicle]]
		+	[[Category: Coatomer]]
		+	[[Category: Copi]]
		+	[[Category: Structural protein]]
		+	[[Category: Transport protein]]

OCA at 15:00, 27 May 2015

OCA — Wed, 27 May 2015 15:00:54 GMT

←Older revision		Revision as of 15:00, 27 May 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5a1u is ON HOLD	+	The entry 5a1u is ON HOLD until Paper Publication

	Authors: Dodonova, S.O., Diestelkoetter-Bachert, P., von Appen, A., Hagen, W.J.H., Beck, R., Beck, M., Wieland, F., Briggs, J.A.G.		Authors: Dodonova, S.O., Diestelkoetter-Bachert, P., von Appen, A., Hagen, W.J.H., Beck, R., Beck, M., Wieland, F., Briggs, J.A.G.