5zoj - Revision history

OCA at 10:28, 27 March 2024

2024-03-27T10:28:48Z

←Older revision		Revision as of 10:28, 27 March 2024
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	==Crystal structure of human SMAD2-MAN1 complex==		==Crystal structure of human SMAD2-MAN1 complex==
-	<StructureSection load='5zoj' size='340' side='right' caption='[[5zoj]], [[Resolution\|resolution]] 2.79Å' scene=''>	+	<StructureSection load='5zoj' size='340' side='right'caption='[[5zoj]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zoj]] is a 5 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=5ZOJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ZOJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zoj]] is a 5 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=5ZOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZOJ FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>SMAD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])~~, ~~MAN1 (~~[~~http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.794Å</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=5zoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoj OCA], [~~http~~://pdbe.org/5zoj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5zoj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5zoj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoj 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=5zoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoj OCA], [https://pdbe.org/5zoj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zoj RCSB], [https://www.ebi.ac.uk/pdbsum/5zoj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoj ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/MAN1_HUMAN MAN1_HUMAN]] Isolated osteopoikilosis;Buschke-Ollendorff syndrome;12q14 microdeletion syndrome;Melorheostosis with osteopoikilosis. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SMAD2_HUMAN SMAD2_HUMAN]] Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.<ref>PMID:9892009</ref> <ref>PMID:16751101</ref> <ref>PMID:17327236</ref> <ref>PMID:16862174</ref> <ref>PMID:19289081</ref> [[http://www.uniprot.org/uniprot/MAN1_HUMAN MAN1_HUMAN]] Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest.<ref>PMID:15601644</ref> <ref>PMID:15647271</ref>	+	[https://www.uniprot.org/uniprot/SMAD2_HUMAN SMAD2_HUMAN] Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.<ref>PMID:9892009</ref> <ref>PMID:16751101</ref> <ref>PMID:17327236</ref> <ref>PMID:16862174</ref> <ref>PMID:19289081</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Receptor-regulated SMAD (R-SMAD: SMAD1, SMAD2, SMAD3, SMAD5 and SMAD8) proteins are key transcription factors of the transforming growth factor-beta (TGF-beta) superfamily of cytokines. MAN1, an integral protein of the inner nuclear membrane, is a SMAD cofactor that terminates TGF-beta superfamily signals. Heterozygous loss-of-function mutations in MAN1 result in osteopoikilosis, Buschke-Ollendorff syndrome and melorheostosis. MAN1 interacts with MAD homology 2 (MH2) domains of R-SMAD proteins using its C-terminal U2AF homology motif (UHM) domain and UHM ligand motif (ULM) and facilitates R-SMAD dephosphorylation. Here, we report the structural basis for R-SMAD recognition by MAN1. The SMAD2-MAN1 and SMAD1-MAN1 complex structures show that an intramolecular UHM-ULM interaction of MAN1 forms a hydrophobic surface that interacts with a hydrophobic surface among the H2 helix, the strands beta8 and beta9, and the L3 loop of the MH2 domains of R-SMAD proteins. The complex structures also show the mechanism by which SMAD cofactors distinguish R-SMAD proteins that possess a highly conserved molecular surface.	+
-		+
-	Structural basis for receptor-regulated SMAD recognition by MAN1.,Miyazono KI, Ohno Y, Wada H, Ito T, Fukatsu Y, Kurisaki A, Asashima M, Tanokura M Nucleic Acids Res. 2018 Oct 13. pii: 5128924. doi: 10.1093/nar/gky925. PMID:30321401<ref>PMID:30321401</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5zoj" style="background-color:#fffaf0;"></div~~>	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Ito, T]]	+	[[Category: Large Structures]]
-	[[Category: Miyazono, K]]	+	[[Category: Ito T]]
-	[[Category: Ohno, Y]]	+	[[Category: Miyazono K]]
-	[[Category: Tanokura, M]]	+	[[Category: Ohno Y]]
-	~~[[Category: Complex]]~~	+	[[Category: Tanokura M]]
-	~~[[Category: Dna binding protein]]~~	+
-	~~[[Category: Tgf-beta signaling]]~~	+
-	~~[[Category: Transcription~~]]	+

OCA at 08:54, 14 November 2018

2018-11-14T08:54:11Z

←Older revision		Revision as of 08:54, 14 November 2018
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	<StructureSection load='5zoj' size='340' side='right' caption='[[5zoj]], [[Resolution\|resolution]] 2.79Å' scene=''>		<StructureSection load='5zoj' size='340' side='right' caption='[[5zoj]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5zoj]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZOJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5zoj]] is a 5 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=5ZOJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZOJ FirstGlance]. <br>
-	</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=5zoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoj OCA], [http://pdbe.org/5zoj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zoj RCSB], [http://www.ebi.ac.uk/pdbsum/5zoj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoj ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SMAD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MAN1 ([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=5zoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoj OCA], [http://pdbe.org/5zoj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zoj RCSB], [http://www.ebi.ac.uk/pdbsum/5zoj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoj ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 10:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SMAD2_HUMAN SMAD2_HUMAN]] Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.<ref>PMID:9892009</ref> <ref>PMID:16751101</ref> <ref>PMID:17327236</ref> <ref>PMID:16862174</ref> <ref>PMID:19289081</ref> [[http://www.uniprot.org/uniprot/MAN1_HUMAN MAN1_HUMAN]] Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest.<ref>PMID:15601644</ref> <ref>PMID:15647271</ref>		[[http://www.uniprot.org/uniprot/SMAD2_HUMAN SMAD2_HUMAN]] Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.<ref>PMID:9892009</ref> <ref>PMID:16751101</ref> <ref>PMID:17327236</ref> <ref>PMID:16862174</ref> <ref>PMID:19289081</ref> [[http://www.uniprot.org/uniprot/MAN1_HUMAN MAN1_HUMAN]] Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest.<ref>PMID:15601644</ref> <ref>PMID:15647271</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Receptor-regulated SMAD (R-SMAD: SMAD1, SMAD2, SMAD3, SMAD5 and SMAD8) proteins are key transcription factors of the transforming growth factor-beta (TGF-beta) superfamily of cytokines. MAN1, an integral protein of the inner nuclear membrane, is a SMAD cofactor that terminates TGF-beta superfamily signals. Heterozygous loss-of-function mutations in MAN1 result in osteopoikilosis, Buschke-Ollendorff syndrome and melorheostosis. MAN1 interacts with MAD homology 2 (MH2) domains of R-SMAD proteins using its C-terminal U2AF homology motif (UHM) domain and UHM ligand motif (ULM) and facilitates R-SMAD dephosphorylation. Here, we report the structural basis for R-SMAD recognition by MAN1. The SMAD2-MAN1 and SMAD1-MAN1 complex structures show that an intramolecular UHM-ULM interaction of MAN1 forms a hydrophobic surface that interacts with a hydrophobic surface among the H2 helix, the strands beta8 and beta9, and the L3 loop of the MH2 domains of R-SMAD proteins. The complex structures also show the mechanism by which SMAD cofactors distinguish R-SMAD proteins that possess a highly conserved molecular surface.
		+
		+	Structural basis for receptor-regulated SMAD recognition by MAN1.,Miyazono KI, Ohno Y, Wada H, Ito T, Fukatsu Y, Kurisaki A, Asashima M, Tanokura M Nucleic Acids Res. 2018 Oct 13. pii: 5128924. doi: 10.1093/nar/gky925. PMID:30321401<ref>PMID:30321401</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5zoj" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Ito, T]]		[[Category: Ito, T]]
	[[Category: Miyazono, K]]		[[Category: Miyazono, K]]

OCA at 08:01, 10 October 2018

2018-10-10T08:01:06Z

←Older revision		Revision as of 08:01, 10 October 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The entry ~~5zoj~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Crystal structure of human SMAD2-MAN1 complex==
-		+	<StructureSection load='5zoj' size='340' side='right' caption='[[5zoj]], [[Resolution\|resolution]] 2.79Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5zoj]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZOJ FirstGlance]. <br>
-	~~Description~~:	+	</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=5zoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoj OCA], [http://pdbe.org/5zoj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zoj RCSB], [http://www.ebi.ac.uk/pdbsum/5zoj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoj ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/MAN1_HUMAN MAN1_HUMAN]] Isolated osteopoikilosis;Buschke-Ollendorff syndrome;12q14 microdeletion syndrome;Melorheostosis with osteopoikilosis. The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SMAD2_HUMAN SMAD2_HUMAN]] Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator.<ref>PMID:9892009</ref> <ref>PMID:16751101</ref> <ref>PMID:17327236</ref> <ref>PMID:16862174</ref> <ref>PMID:19289081</ref> [[http://www.uniprot.org/uniprot/MAN1_HUMAN MAN1_HUMAN]] Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest.<ref>PMID:15601644</ref> <ref>PMID:15647271</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ito, T]]
		+	[[Category: Miyazono, K]]
		+	[[Category: Ohno, Y]]
		+	[[Category: Tanokura, M]]
		+	[[Category: Complex]]
		+	[[Category: Dna binding protein]]
		+	[[Category: Tgf-beta signaling]]
		+	[[Category: Transcription]]

OCA at 03:50, 30 May 2018

2018-05-30T03:50:30Z

←Older revision		Revision as of 03:50, 30 May 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors:		Authors:

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

2018-04-18T04:08:12Z

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

←Older revision

Revision as of 04:08, 18 April 2018

OCA: New page: '''Unreleased structure''' The entry 5zoj is ON HOLD Authors: Description: Category: Unreleased Structures

2018-04-18T04:08:11Z

New page: '''Unreleased structure''' The entry 5zoj is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5zoj is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]