5azw - Revision history

OCA at 06:32, 31 May 2023

OCA — Wed, 31 May 2023 06:32:59 GMT

←Older revision		Revision as of 06:32, 31 May 2023
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	<StructureSection load='5azw' size='340' side='right'caption='[[5azw]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='5azw' size='340' side='right'caption='[[5azw]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5azw]] is a 2 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=5AZW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5AZW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5azw]] is a 2 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=5AZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AZW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5azx\|5azx]], [[5azy\|5azy]]</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=5azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azw OCA], [https://pdbe.org/5azw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5azw RCSB], [https://www.ebi.ac.uk/pdbsum/5azw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5azw ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TMED2, RNP24 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=5azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azw OCA], [~~http~~://pdbe.org/5azw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5azw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5azw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5azw ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/TMED2_HUMAN TMED2_HUMAN]] Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing.<ref>PMID:10761932</ref> <ref>PMID:17693410</ref> <ref>PMID:20361938</ref> <ref>PMID:20427317</ref> <ref>PMID:21219331</ref>	+	[https://www.uniprot.org/uniprot/TMED2_HUMAN TMED2_HUMAN] Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing.<ref>PMID:10761932</ref> <ref>PMID:17693410</ref> <ref>PMID:20361938</ref> <ref>PMID:20427317</ref> <ref>PMID:21219331</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__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Nagae, M]]	+	[[Category: Nagae M]]
-	[[Category: Yamaguchi, Y]]	+	[[Category: Yamaguchi Y]]
-	~~[[Category: Gpi-anchored protein]]~~	+
-	~~[[Category: P24 complex]]~~	+
-	~~[[Category: Protein transport~~]]	+

OCA at 09:58, 26 February 2020

OCA — Wed, 26 Feb 2020 09:58:02 GMT

←Older revision		Revision as of 09:58, 26 February 2020
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	==Crystal structure of p24beta1 GOLD domain==		==Crystal structure of p24beta1 GOLD domain==
-	<StructureSection load='5azw' size='340' side='right' caption='[[5azw]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='5azw' size='340' side='right'caption='[[5azw]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5azw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5azw]] is a 2 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=5AZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5azx\|5azx]], [[5azy\|5azy]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5azx\|5azx]], [[5azy\|5azy]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TMED2, RNP24 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azw OCA], [http://pdbe.org/5azw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5azw RCSB], [http://www.ebi.ac.uk/pdbsum/5azw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5azw 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=5azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azw OCA], [http://pdbe.org/5azw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5azw RCSB], [http://www.ebi.ac.uk/pdbsum/5azw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5azw ProSAT]</span></td></tr>
	</table>		</table>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Nagae, M]]		[[Category: Nagae, M]]
	[[Category: Yamaguchi, Y]]		[[Category: Yamaguchi, Y]]

OCA at 15:11, 14 September 2016

OCA — Wed, 14 Sep 2016 15:11:13 GMT

←Older revision		Revision as of 15:11, 14 September 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5azw is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal structure of p24beta1 GOLD domain==
		+	<StructureSection load='5azw' size='340' side='right' caption='[[5azw]], [[Resolution\|resolution]] 1.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5azw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AZW FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5azx\|5azx]], [[5azy\|5azy]]</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=5azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5azw OCA], [http://pdbe.org/5azw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5azw RCSB], [http://www.ebi.ac.uk/pdbsum/5azw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5azw ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TMED2_HUMAN TMED2_HUMAN]] Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway but also in post-Golgi membranes. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side. In COPII vesicle-mediated anterograde transport involved in the transport of GPI-anchored proteins and proposed to act together with TMED10 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER. Recognizes GPI anchors structural remodeled in the ER by PGAP1 and MPPE1. In COPI vesicle-mediated retrograde transport inhibits the GTPase-activating activity of ARFGAP1 towards ARF1 thus preventing immature uncoating and allowing cargo selection to take place. Involved in trafficking of G protein-coupled receptors (GPCRs). Regulates F2RL1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the plasma membrane thus contributing to receptor resensitization. Facilitates CASR maturation and stabilization in the early secretory pathway and increases CASR plasma membrane targeting. Proposed to be involved in organization of intracellular membranes such as the maintenance of the Golgi apparatus. May also play a role in the biosynthesis of secreted cargo such as eventual processing.<ref>PMID:10761932</ref> <ref>PMID:17693410</ref> <ref>PMID:20361938</ref> <ref>PMID:20427317</ref> <ref>PMID:21219331</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The p24 family consists of four subfamilies (p24alpha, p24beta, p24gamma, and p24delta), and the proteins are thought to form hetero-oligomeric complexes for efficient transport of cargo proteins from the endoplasmic reticulum to the Golgi apparatus. The proteins possess a conserved luminal Golgi dynamics (GOLD) domain, whose functions are largely unknown. Here, we present structural and biochemical studies of p24beta1 and p24delta1 GOLD domains. Use of GOLD domain-deleted mutants revealed that the GOLD domain of p24delta1 is required for proper p24 hetero-oligomeric complex formation and efficient transport of GPI-anchored proteins. The p24beta1 and p24delta1 GOLD domains share a common beta-sandwich fold with a characteristic intrasheet disulfide bond. The GOLD domain of p24delta1 crystallized as dimers, allowing the analysis of a homophilic interaction site. Surface plasmon resonance and solution NMR analyses revealed that p24beta1 and p24delta1 GOLD domains interact weakly (Kd= ~10-4M). Bi-protein titration provided interaction site maps. We propose that the heterophilic interaction of p24 GOLD domains contributes to the formation of the p24 hetero-oligomeric complex and to efficient cargo transport.

-	~~Authors~~:	+	3D Structure and Interaction of p24beta and p24delta Golgi Dynamics Domains: Implication for p24 Complex Formation and Cargo Transport.,Nagae M, Hirata T, Morita-Matsumoto K, Theiler R, Fujita M, Kinoshita T, Yamaguchi Y J Mol Biol. 2016 Aug 25. pii: S0022-2836(16)30342-4. doi:, 10.1016/j.jmb.2016.08.023. PMID:27569046<ref>PMID:27569046</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5azw" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Nagae, M]]
		+	[[Category: Yamaguchi, Y]]
		+	[[Category: Gpi-anchored protein]]
		+	[[Category: P24 complex]]
		+	[[Category: Protein transport]]

OCA at 11:01, 15 May 2016

OCA — Sun, 15 May 2016 11:01:53 GMT

←Older revision		Revision as of 11:01, 15 May 2016
Line 3:		Line 3:
	The entry 5azw is ON HOLD until Paper Publication		The entry 5azw is ON HOLD until Paper Publication

-	Authors: ~~Nagae, M., Yamaguchi, Y.~~	+	Authors:

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Nagae, M]]
-	[[Category: Yamaguchi, Y]]

OCA: Protected "5azw" [edit=sysop:move=sysop]

OCA — Tue, 01 Dec 2015 00:45:31 GMT

Protected "5azw" [edit=sysop:move=sysop]

←Older revision

Revision as of 00:45, 1 December 2015

OCA: New page: '''Unreleased structure''' The entry 5azw is ON HOLD until Paper Publication Authors: Nagae, M., Yamaguchi, Y. Description: Category: Unreleased Structures Category: Nagae, M ...

OCA — Tue, 01 Dec 2015 00:45:30 GMT

New page: '''Unreleased structure''' The entry 5azw is ON HOLD until Paper Publication Authors: Nagae, M., Yamaguchi, Y. Description: Category: Unreleased Structures Category: Nagae, M ...

New page

'''Unreleased structure'''

The entry 5azw is ON HOLD until Paper Publication

Authors: Nagae, M., Yamaguchi, Y.

Description:
[[Category: Unreleased Structures]]
[[Category: Nagae, M]]
[[Category: Yamaguchi, Y]]