5g1e - Revision history

OCA at 13:35, 26 July 2023

2023-07-26T13:35:10Z

←Older revision		Revision as of 13:35, 26 July 2023
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	<StructureSection load='5g1e' size='340' side='right'caption='[[5g1e]], [[Resolution\|resolution]] 1.92Å' scene=''>		<StructureSection load='5g1e' size='340' side='right'caption='[[5g1e]], [[Resolution\|resolution]] 1.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5g1e]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5G1E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5g1e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G1E FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">[[~~5g1d~~\|~~5g1d~~]]</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]] 1.92Å</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=5g1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1e OCA], [~~http~~://pdbe.org/5g1e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5g1e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5g1e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1e 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=5g1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1e OCA], [https://pdbe.org/5g1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g1e RCSB], [https://www.ebi.ac.uk/pdbsum/5g1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SDCB1_RAT SDCB1_RAT]] Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis. Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway.[UniProtKB:O00560]	+	[https://www.uniprot.org/uniprot/SDCB1_RAT SDCB1_RAT] Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis. Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway.[UniProtKB:O00560]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 5g1e" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5g1e" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[3D structures of syntenin\|3D structures of syntenin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Kim, H~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Lee, I~~]]	+	[[Category: Kim H]]
-	[[Category: Lee~~, W~~]]	+	[[Category: Lee I]]
-	[[Category: ~~Yun, J H~~]]	+	[[Category: Lee W]]
-	[[Category: ~~Signaling protein~~]]	+	[[Category: Yun JH]]

OCA at 06:34, 13 May 2020

2020-05-13T06:34:41Z

←Older revision		Revision as of 06:34, 13 May 2020
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	==The complex structure of syntenin-1 PDZ domain with c-terminal extension==		==The complex structure of syntenin-1 PDZ domain with c-terminal extension==
-	<StructureSection load='5g1e' size='340' side='right' caption='[[5g1e]], [[Resolution\|resolution]] 1.92Å' scene=''>	+	<StructureSection load='5g1e' size='340' side='right'caption='[[5g1e]], [[Resolution\|resolution]] 1.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5g1e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1E OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5G1E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5g1e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5G1E FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5g1d\|5g1d]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5g1d\|5g1d]]</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=5g1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1e OCA], [http://pdbe.org/5g1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g1e RCSB], [http://www.ebi.ac.uk/pdbsum/5g1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1e 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=5g1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1e OCA], [http://pdbe.org/5g1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g1e RCSB], [http://www.ebi.ac.uk/pdbsum/5g1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1e ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
		+	[[Category: Large Structures]]
	[[Category: Kim, H]]		[[Category: Kim, H]]
	[[Category: Lee, I]]		[[Category: Lee, I]]

OCA at 10:51, 10 December 2016

2016-12-10T10:51:31Z

←Older revision		Revision as of 10:51, 10 December 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The ~~entry~~ 5g1e is ~~ON HOLD until Paper~~ Publication	+	==The complex structure of syntenin-1 PDZ domain with c-terminal extension==
		+	<StructureSection load='5g1e' size='340' side='right' caption='[[5g1e]], [[Resolution\|resolution]] 1.92Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5g1e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G1E FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5g1d\|5g1d]]</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=5g1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1e OCA], [http://pdbe.org/5g1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g1e RCSB], [http://www.ebi.ac.uk/pdbsum/5g1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1e ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SDCB1_RAT SDCB1_RAT]] Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1. In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis. Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway.[UniProtKB:O00560]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The PDZ domain-containing scaffold protein, syntenin-1, binds to the transmembrane proteoglycan, syndecan-4, but the molecular mechanism/function of this interaction are unknown. Crystal structure analysis of syntenin-1/syndecan-4 cytoplasmic domains revealed that syntenin-1 forms a symmetrical pair of dimers anchored by a syndecan-4 dimer. The syndecan-4 cytoplasmic domain is a compact intertwined dimer with a symmetrical clamp shape and two antiparallel strands forming a cavity within the dimeric twist. The PDZ2 domain of syntenin-1 forms a direct antiparallel interaction with the syndecan-4 cytoplasmic domain, inhibiting the functions of syndecan-4 such as focal adhesion formation. Moreover, C-terminal region of syntenin-1 reveals an essential role for enhancing the molecular homodimerization. Mutation of key syntenin-1 residues involved in the syndecan-4 interaction or homodimer formation abolishes the inhibitory function of syntenin-1, as does deletion of the homodimerization-related syntenin-1 C-terminal domain. Syntenin-1, but not dimer-formation-incompetent mutants, rescued the syndecan-4-mediated inhibition of migration and pulmonary metastasis by B16F10 cells. Therefore, we conclude that syntenin-1 negatively regulates syndecan-4 function via oligomerization and/or syndecan-4 interaction, impacting cytoskeletal organization and cell migration.

-	~~Authors: Lee~~, I., ~~Kim, H.~~, Yun, J~~.H.~~, Lee, W.	+	New structural insight of C-terminal region of Syntenin-1, enhancing the molecular dimerization and inhibitory function related on Syndecan-4 signaling.,Choi Y, Yun JH, Yoo J, Lee I, Kim H, Son HN, Kim IS, Yoon HS, Zimmermann P, Couchman JR, Cho HS, Oh ES, Lee W Sci Rep. 2016 Nov 10;6:36818. doi: 10.1038/srep36818. PMID:27830760<ref>PMID:27830760</ref>

-	~~Description: The complex structure~~ of ~~syntenin~~-~~1 PDZ domain with c~~-~~terminal extension~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category~~: ~~Unreleased Structures]]~~	+	</div>
-	~~[[Category: Lee, W]]~~	+	<div class="pdbe-citations 5g1e" style="background-color:#fffaf0;"></div>
-	~~[[Category: Yun, J.H]]~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Kim, H]]		[[Category: Kim, H]]
	[[Category: Lee, I]]		[[Category: Lee, I]]
		+	[[Category: Lee, W]]
		+	[[Category: Yun, J H]]
		+	[[Category: Signaling protein]]

OCA: Protected "5g1e" [edit=sysop:move=sysop]

2016-05-10T23:20:54Z

Protected "5g1e" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:20, 10 May 2016

OCA: New page: '''Unreleased structure''' The entry 5g1e is ON HOLD until Paper Publication Authors: Lee, I., Kim, H., Yun, J.H., Lee, W. Description: The complex structure of syntenin-1 PDZ domain w...

2016-05-10T23:20:53Z

New page: '''Unreleased structure''' The entry 5g1e is ON HOLD until Paper Publication Authors: Lee, I., Kim, H., Yun, J.H., Lee, W. Description: The complex structure of syntenin-1 PDZ domain w...

New page

'''Unreleased structure'''

The entry 5g1e is ON HOLD until Paper Publication

Authors: Lee, I., Kim, H., Yun, J.H., Lee, W.

Description: The complex structure of syntenin-1 PDZ domain with c-terminal extension
[[Category: Unreleased Structures]]
[[Category: Lee, W]]
[[Category: Yun, J.H]]
[[Category: Kim, H]]
[[Category: Lee, I]]