4kmh - Revision history

OCA at 14:30, 8 November 2023

2023-11-08T14:30:45Z

←Older revision		Revision as of 14:30, 8 November 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4kmh]] 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=4KMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KMH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4kmh]] 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=4KMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KMH 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=4kmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmh OCA], [https://pdbe.org/4kmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kmh RCSB], [https://www.ebi.ac.uk/pdbsum/4kmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kmh ProSAT]</span></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]] 3.04Å</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=4kmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmh OCA], [https://pdbe.org/4kmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kmh RCSB], [https://www.ebi.ac.uk/pdbsum/4kmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kmh ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 08:59, 7 December 2022

2022-12-07T08:59:51Z

←Older revision		Revision as of 08:59, 7 December 2022
Line 1:		Line 1:

	==Crystal structure of Suppressor of Fused d20==		==Crystal structure of Suppressor of Fused d20==
-	<StructureSection load='4kmh' size='340' side='right' caption='[[4kmh]], [[Resolution\|resolution]] 3.04Å' scene=''>	+	<StructureSection load='4kmh' size='340' side='right'caption='[[4kmh]], [[Resolution\|resolution]] 3.04Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4kmh]] 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=4KMH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4KMH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4kmh]] 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=4KMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KMH FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4km8\|4km8]], [[4km9\|4km9]], [[4kma\|4kma]], [[4kmd\|4kmd]]</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=4kmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmh OCA], [https://pdbe.org/4kmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kmh RCSB], [https://www.ebi.ac.uk/pdbsum/4kmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kmh ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUFU, UNQ650/PRO1280 ([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=4kmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmh OCA], [~~http~~://pdbe.org/4kmh PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4kmh RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4kmh PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4kmh ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/SUFU_HUMAN SUFU_HUMAN]] Defects in SUFU are a cause of medulloblastoma (MDB) [MIM:[~~http~~://omim.org/entry/155255 155255]]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Defects in SUFU play a role in predisposition to desmoplastic MDB. These tumors make up about 20 to 30% of medulloblastomas, have a more nodular architecture than 'classical' medulloblastoma, and may have a better prognosis.	+	[https://www.uniprot.org/uniprot/SUFU_HUMAN SUFU_HUMAN] Defects in SUFU are a cause of medulloblastoma (MDB) [MIM:[https://omim.org/entry/155255 155255]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Defects in SUFU play a role in predisposition to desmoplastic MDB. These tumors make up about 20 to 30% of medulloblastomas, have a more nodular architecture than 'classical' medulloblastoma, and may have a better prognosis.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SUFU_HUMAN SUFU_HUMAN]] Negative regulator in the hedgehog signaling pathway. Down-regulates GLI1-mediated transactivation of target genes. Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein. Negative regulator of beta-catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A).<ref>PMID:10564661</ref> <ref>PMID:10559945</ref> <ref>PMID:12068298</ref> <ref>PMID:10806483</ref> <ref>PMID:22365972</ref>	+	[https://www.uniprot.org/uniprot/SUFU_HUMAN SUFU_HUMAN] Negative regulator in the hedgehog signaling pathway. Down-regulates GLI1-mediated transactivation of target genes. Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein. Negative regulator of beta-catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A).<ref>PMID:10564661</ref> <ref>PMID:10559945</ref> <ref>PMID:12068298</ref> <ref>PMID:10806483</ref> <ref>PMID:22365972</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Qi, X]]	+	[[Category: Large Structures]]
-	[[Category: Wu, G]]	+	[[Category: Qi X]]
-	[[Category: Zhang, Y]]	+	[[Category: Wu G]]
-	[[Category: Zhang, Z]]	+	[[Category: Zhang Y]]
-	~~[[Category: Helix and beta strand]]~~	+	[[Category: Zhang Z]]
-	~~[[Category: Protein binding~~]]	+

OCA at 16:10, 5 August 2016

2016-08-05T16:10:07Z

←Older revision		Revision as of 16:10, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Suppressor of Fused d20==		==Crystal structure of Suppressor of Fused d20==
	<StructureSection load='4kmh' size='340' side='right' caption='[[4kmh]], [[Resolution\|resolution]] 3.04Å' scene=''>		<StructureSection load='4kmh' size='340' side='right' caption='[[4kmh]], [[Resolution\|resolution]] 3.04Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4km8\|4km8]], [[4km9\|4km9]], [[4kma\|4kma]], [[4kmd\|4kmd]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4km8\|4km8]], [[4km9\|4km9]], [[4kma\|4kma]], [[4kmd\|4kmd]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUFU, UNQ650/PRO1280 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUFU, UNQ650/PRO1280 ([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=4kmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kmh RCSB], [http://www.ebi.ac.uk/pdbsum/4kmh 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=4kmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmh OCA], [http://pdbe.org/4kmh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kmh RCSB], [http://www.ebi.ac.uk/pdbsum/4kmh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kmh ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	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 4kmh" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:48, 21 December 2014

2014-12-21T16:48:58Z

←Older revision		Revision as of 16:48, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4kmh\| PDB=4kmh \| SCENE= }}~~	+	==Crystal structure of Suppressor of Fused d20==
-	===Crystal structure of Suppressor of Fused d20===	+	<StructureSection load='4kmh' size='340' side='right' caption='[[4kmh]], [[Resolution\|resolution]] 3.04Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24217340}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4kmh]] 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=4KMH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KMH FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4km8\|4km8]], [[4km9\|4km9]], [[4kma\|4kma]], [[4kmd\|4kmd]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUFU, UNQ650/PRO1280 ([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=4kmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kmh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kmh RCSB], [http://www.ebi.ac.uk/pdbsum/4kmh PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/SUFU_HUMAN SUFU_HUMAN]] Defects in SUFU are a cause of medulloblastoma (MDB) [MIM:[http://omim.org/entry/155255 155255]]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Defects in SUFU play a role in predisposition to desmoplastic MDB. These tumors make up about 20 to 30% of medulloblastomas, have a more nodular architecture than 'classical' medulloblastoma, and may have a better prognosis.		[[http://www.uniprot.org/uniprot/SUFU_HUMAN SUFU_HUMAN]] Defects in SUFU are a cause of medulloblastoma (MDB) [MIM:[http://omim.org/entry/155255 155255]]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Defects in SUFU play a role in predisposition to desmoplastic MDB. These tumors make up about 20 to 30% of medulloblastomas, have a more nodular architecture than 'classical' medulloblastoma, and may have a better prognosis.
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/SUFU_HUMAN SUFU_HUMAN]] Negative regulator in the hedgehog signaling pathway. Down-regulates GLI1-mediated transactivation of target genes. Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein. Negative regulator of beta-catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A).<ref>PMID:10564661</ref> <ref>PMID:10559945</ref> <ref>PMID:12068298</ref> <ref>PMID:10806483</ref> <ref>PMID:22365972</ref>		[[http://www.uniprot.org/uniprot/SUFU_HUMAN SUFU_HUMAN]] Negative regulator in the hedgehog signaling pathway. Down-regulates GLI1-mediated transactivation of target genes. Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein. Negative regulator of beta-catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A).<ref>PMID:10564661</ref> <ref>PMID:10559945</ref> <ref>PMID:12068298</ref> <ref>PMID:10806483</ref> <ref>PMID:22365972</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Hedgehog (Hh) signalling regulates embryonic development and adult tissue homoeostasis. Mutations of its pathway components including Suppressor of Fused (Sufu) and Gli/Ci predispose to cancers and congenital anomalies. The Sufu-Gli protein complex occupies a central position in the vertebrate Hh signalling pathway, especially in mammals. Here structures of full-length human and Drosophila Sufu, the human Sufu-Gli complex, along with normal mode analysis and FRET measurement results, reveal that Sufu alternates between 'open' and 'closed' conformations. The 'closed' form of Sufu is stabilized by Gli binding and inhibited by Hh treatment, whereas the 'open' state of Sufu is promoted by Gli-dissociation and Hh signalling. Mutations of critical interface residues disrupt the Sufu-Gli complex and prevent Sufu from repressing Gli-mediated transcription, tethering Gli in the cytoplasm and protecting Gli from the 26S proteasome-mediated degradation. Our study thus provides mechanistic insight into the mutual recognition and regulation between Sufu and Gli/Ci.

-	~~==About this Structure==~~	+	Structural insight into the mutual recognition and regulation between Suppressor of Fused and Gli/Ci.,Zhang Y, Fu L, Qi X, Zhang Z, Xia Y, Jia J, Jiang J, Zhao Y, Wu G Nat Commun. 2013;4:2608. doi: 10.1038/ncomms3608. PMID:24217340<ref>PMID:24217340</ref>
-	~~[[4kmh]] 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=4KMH OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024217340</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Qi, X.]]	+	[[Category: Qi, X]]
-	[[Category: Wu, G.]]	+	[[Category: Wu, G]]
-	[[Category: Zhang, Y.]]	+	[[Category: Zhang, Y]]
-	[[Category: Zhang, Z.]]	+	[[Category: Zhang, Z]]
	[[Category: Helix and beta strand]]		[[Category: Helix and beta strand]]
	[[Category: Protein binding]]		[[Category: Protein binding]]

OCA at 04:28, 13 February 2014

2014-02-13T04:28:49Z

←Older revision		Revision as of 04:28, 13 February 2014
Line 1:		Line 1:
	{{STRUCTURE_4kmh\| PDB=4kmh \| SCENE= }}		{{STRUCTURE_4kmh\| PDB=4kmh \| SCENE= }}
	===Crystal structure of Suppressor of Fused d20===		===Crystal structure of Suppressor of Fused d20===
		+	{{ABSTRACT_PUBMED_24217340}}

	==Disease==		==Disease==
Line 12:		Line 13:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024217340</ref><references group="xtra"/><references/>
	[[Category: Human]]		[[Category: Human]]
	[[Category: Qi, X.]]		[[Category: Qi, X.]]

OCA at 08:48, 27 November 2013

2013-11-27T08:48:04Z

←Older revision		Revision as of 08:48, 27 November 2013
Line 9:		Line 9:

	==About this Structure==		==About this Structure==
-	[[4kmh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KMH OCA].	+	[[4kmh]] 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=4KMH OCA].

	==Reference==		==Reference==
	<references group="xtra"/><references/>		<references group="xtra"/><references/>
		+	[[Category: Human]]
	[[Category: Qi, X.]]		[[Category: Qi, X.]]
	[[Category: Wu, G.]]		[[Category: Wu, G.]]

OCA at 13:44, 20 November 2013

2013-11-20T13:44:30Z

←Older revision		Revision as of 13:44, 20 November 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4kmh\| PDB=4kmh \| SCENE= }}
		+	===Crystal structure of Suppressor of Fused d20===

-	~~The~~ entry ~~4kmh~~ is ~~ON HOLD until Paper Publication~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/SUFU_HUMAN SUFU_HUMAN]] Defects in SUFU are a cause of medulloblastoma (MDB) [MIM:[http://omim.org/entry/155255 155255]]. MDB is a malignant, invasive embryonal tumor of the cerebellum with a preferential manifestation in children. Defects in SUFU play a role in predisposition to desmoplastic MDB. These tumors make up about 20 to 30% of medulloblastomas, have a more nodular architecture than 'classical' medulloblastoma, and may have a better prognosis.

-	~~Authors~~: ~~Zhang, Y~~., Qi, X., ~~Zhang~~, Z., Wu, G.	+	==Function==
		+	[[http://www.uniprot.org/uniprot/SUFU_HUMAN SUFU_HUMAN]] Negative regulator in the hedgehog signaling pathway. Down-regulates GLI1-mediated transactivation of target genes. Part of a corepressor complex that acts on DNA-bound GLI1. May also act by linking GLI1 to BTRC and thereby targeting GLI1 to degradation by the proteasome. Sequesters GLI1, GLI2 and GLI3 in the cytoplasm, this effect is overcome by binding of STK36 to both SUFU and a GLI protein. Negative regulator of beta-catenin signaling. Regulates the formation of either the repressor form (GLI3R) or the activator form (GLI3A) of the full length form of GLI3 (GLI3FL). GLI3FL is complexed with SUFU in the cytoplasm and is maintained in a neutral state. Without the Hh signal, the SUFU-GLI3 complex is recruited to cilia, leading to the efficient processing of GLI3FL into GLI3R. When Hh signaling is initiated, SUFU dissociates from GLI3FL and the latter translocates to the nucleus, where it is phosphorylated, destabilized, and converted to a transcriptional activator (GLI3A).<ref>PMID:10564661</ref> <ref>PMID:10559945</ref> <ref>PMID:12068298</ref> <ref>PMID:10806483</ref> <ref>PMID:22365972</ref>

-	~~Description: Crystal~~ structure ~~of Suppressor of Fused d20~~	+	==About this Structure==
		+	[[4kmh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KMH OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Qi, X.]]
		+	[[Category: Wu, G.]]
		+	[[Category: Zhang, Y.]]
		+	[[Category: Zhang, Z.]]
		+	[[Category: Helix and beta strand]]
		+	[[Category: Protein binding]]

OCA at 11:45, 19 June 2013

2013-06-19T11:45:37Z

←Older revision		Revision as of 11:45, 19 June 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4kmh is ON HOLD	+	The entry 4kmh is ON HOLD until Paper Publication

-	Authors: ~~zhang~~, ~~yan~~, Qi, ~~xiaolong~~, Zhang, ~~Zhenyi~~, Wu, ~~Geng~~	+	Authors: Zhang, Y., Qi, X., Zhang, Z., Wu, G.

	Description: Crystal structure of Suppressor of Fused d20		Description: Crystal structure of Suppressor of Fused d20

OCA: Protected "4kmh" [edit=sysop:move=sysop]

2013-05-16T06:59:58Z

Protected "4kmh" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:59, 16 May 2013

OCA: New page: '''Unreleased structure''' The entry 4kmh is ON HOLD Authors: zhang, yan, Qi, xiaolong, Zhang, Zhenyi, Wu, Geng Description: Crystal structure of Suppressor of Fused d20

2013-05-16T06:59:57Z

New page: '''Unreleased structure''' The entry 4kmh is ON HOLD Authors: zhang, yan, Qi, xiaolong, Zhang, Zhenyi, Wu, Geng Description: Crystal structure of Suppressor of Fused d20

New page

'''Unreleased structure'''

The entry 4kmh is ON HOLD

Authors: zhang, yan, Qi, xiaolong, Zhang, Zhenyi, Wu, Geng

Description: Crystal structure of Suppressor of Fused d20