4m91 - Revision history

OCA at 16:34, 20 September 2023

OCA — Wed, 20 Sep 2023 16:34:19 GMT

←Older revision		Revision as of 16:34, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4m91]] 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=4M91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M91 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4m91]] 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=4M91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M91 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=4m91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m91 OCA], [https://pdbe.org/4m91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m91 RCSB], [https://www.ebi.ac.uk/pdbsum/4m91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m91 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]] 1.1Å</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=4m91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m91 OCA], [https://pdbe.org/4m91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m91 RCSB], [https://www.ebi.ac.uk/pdbsum/4m91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m91 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 11:03, 21 December 2022

OCA — Wed, 21 Dec 2022 11:03:49 GMT

←Older revision		Revision as of 11:03, 21 December 2022
Line 1:		Line 1:

	==crystal structure of hN33/Tusc3-peptide 1==		==crystal structure of hN33/Tusc3-peptide 1==
-	<StructureSection load='4m91' size='340' side='right' caption='[[4m91]], [[Resolution\|resolution]] 1.10Å' scene=''>	+	<StructureSection load='4m91' size='340' side='right'caption='[[4m91]], [[Resolution\|resolution]] 1.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4m91]] 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=4M91 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4M91 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4m91]] 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=4M91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M91 FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m92\|4m92]]</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=4m91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m91 OCA], [https://pdbe.org/4m91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m91 RCSB], [https://www.ebi.ac.uk/pdbsum/4m91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m91 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TUSC3, N33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CRBN, AD-006 ([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=4m91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m91 OCA], [~~http~~://pdbe.org/4m91 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4m91 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4m91 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4m91 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN~~]] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/CRBN_HUMAN CRBN_HUMAN]~~] Autosomal recessive nonsyndromic intellectual deficit~~;Distal monosomy 3p~~. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Magnesium transporter. May be involved in N-glycosylation through its association with N-oligosaccharyl transferase.<ref>PMID:19717468</ref> [[http://www.uniprot.org/uniprot/CRBN_HUMAN CRBN_HUMAN]] Component of some DCX (DDB1-CUL4-X-box) E3 protein ligase complex, a complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins and is required for limb outgrowth and expression of the fibroblast growth factor FGF8. In the complex, may act as a substrate receptor. Regulates the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1.<ref>PMID:18414909</ref> <ref>PMID:20223979</ref>	+	[https://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN] Magnesium transporter. May be involved in N-glycosylation through its association with N-oligosaccharyl transferase.<ref>PMID:19717468</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: Aebi, M]]	+	[[Category: Large Structures]]
-	[[Category: Brozzo~~, M S~~]]	+	[[Category: Aebi M]]
-	[[Category: Glockshuber, R]]	+	[[Category: Brozzo MS]]
-	[[Category: Malojcic, G]]	+	[[Category: Glockshuber R]]
-	[[Category: Mohorko, E]]	+	[[Category: Malojcic G]]
-	[[Category: Owen~~, R L]]~~	+	[[Category: Mohorko E]]
-	~~[[Category: Endoplasmic reticulum]]~~	+	[[Category: Owen RL]]
-	~~[[Category: Formation of mixed disulfide]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Thioredoxin-like fold~~]]	+

OCA at 13:37, 11 August 2016

OCA — Thu, 11 Aug 2016 13:37:55 GMT

←Older revision		Revision as of 13:37, 11 August 2016
Line 1:		Line 1:
		+
	==crystal structure of hN33/Tusc3-peptide 1==		==crystal structure of hN33/Tusc3-peptide 1==
	<StructureSection load='4m91' size='340' side='right' caption='[[4m91]], [[Resolution\|resolution]] 1.10Å' scene=''>		<StructureSection load='4m91' size='340' side='right' caption='[[4m91]], [[Resolution\|resolution]] 1.10Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m92\|4m92]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m92\|4m92]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TUSC3, N33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CRBN, AD-006 ([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">TUSC3, N33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CRBN, AD-006 ([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=4m91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m91 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m91 RCSB], [http://www.ebi.ac.uk/pdbsum/4m91 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=4m91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m91 OCA], [http://pdbe.org/4m91 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m91 RCSB], [http://www.ebi.ac.uk/pdbsum/4m91 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m91 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 4m91" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:28, 5 January 2015

OCA — Mon, 05 Jan 2015 09:28:10 GMT

←Older revision		Revision as of 09:28, 5 January 2015
Line 2:		Line 2:
	<StructureSection load='4m91' size='340' side='right' caption='[[4m91]], [[Resolution\|resolution]] 1.10Å' scene=''>		<StructureSection load='4m91' size='340' side='right' caption='[[4m91]], [[Resolution\|resolution]] 1.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4m91]] 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=4M91 OCA]. <br>	+	<table><tr><td colspan='2'>[[4m91]] 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=4M91 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M91 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m92\|4m92]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m92\|4m92]]</td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TUSC3, N33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CRBN, AD-006 ([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">TUSC3, N33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CRBN, AD-006 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr~~><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class~~='~~plainlinks~~'~~>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=4m91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m91 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m91 RCSB], [http://www.ebi.ac.uk/pdbsum/4m91 PDBsum]</span></td></tr>
-	~~<tr~~><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4m91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m91 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m91 RCSB], [http://www.ebi.ac.uk/pdbsum/4m91 PDBsum]</span></td></tr>	+	</table>
-	<table>	+
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/CRBN_HUMAN CRBN_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit;Distal monosomy 3p. The disease is caused by mutations affecting the gene represented in this entry.		[[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/CRBN_HUMAN CRBN_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit;Distal monosomy 3p. The disease is caused by mutations affecting the gene represented in this entry.
Line 18:		Line 17:
	Structural basis of substrate specificity of human oligosaccharyl transferase subunit n33/tusc3 and its role in regulating protein N-glycosylation.,Mohorko E, Owen RL, Malojcic G, Brozzo MS, Aebi M, Glockshuber R Structure. 2014 Apr 8;22(4):590-601. doi: 10.1016/j.str.2014.02.013. Epub 2014, Mar 27. PMID:24685145<ref>PMID:24685145</ref>		Structural basis of substrate specificity of human oligosaccharyl transferase subunit n33/tusc3 and its role in regulating protein N-glycosylation.,Mohorko E, Owen RL, Malojcic G, Brozzo MS, Aebi M, Glockshuber R Structure. 2014 Apr 8;22(4):590-601. doi: 10.1016/j.str.2014.02.013. Epub 2014, Mar 27. PMID:24685145<ref>PMID:24685145</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
	== References ==		== References ==
Line 25:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Aebi, M.]]	+	[[Category: Aebi, M]]
-	[[Category: Brozzo, M S.]]	+	[[Category: Brozzo, M S]]
-	[[Category: Glockshuber, R.]]	+	[[Category: Glockshuber, R]]
-	[[Category: Malojcic, G.]]	+	[[Category: Malojcic, G]]
-	[[Category: Mohorko, E.]]	+	[[Category: Mohorko, E]]
-	[[Category: Owen, R L.]]	+	[[Category: Owen, R L]]
	[[Category: Endoplasmic reticulum]]		[[Category: Endoplasmic reticulum]]
	[[Category: Formation of mixed disulfide]]		[[Category: Formation of mixed disulfide]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Thioredoxin-like fold]]		[[Category: Thioredoxin-like fold]]

OCA at 07:00, 7 May 2014

OCA — Wed, 07 May 2014 07:00:23 GMT

←Older revision		Revision as of 07:00, 7 May 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4m91\| PDB~~=4m91 \| ~~SCENE~~= }}	+	==crystal structure of hN33/Tusc3-peptide 1==
-	===~~crystal~~ structure ~~of hN33~~/~~Tusc3~~-~~peptide~~ 1===	+	<StructureSection load='4m91' size='340' side='right' caption='[[4m91]], [[Resolution\|resolution]] 1.10Å' scene=''>
-		+	== Structural highlights ==
-	==Disease==	+	<table><tr><td colspan='2'>[[4m91]] 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=4M91 OCA]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m92\|4m92]]</td></tr>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">TUSC3, N33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CRBN, AD-006 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4m91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m91 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m91 RCSB], [http://www.ebi.ac.uk/pdbsum/4m91 PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/CRBN_HUMAN CRBN_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit;Distal monosomy 3p. The disease is caused by mutations affecting the gene represented in this entry.		[[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/CRBN_HUMAN CRBN_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit;Distal monosomy 3p. The disease is caused by mutations affecting the gene represented in this entry.
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Magnesium transporter. May be involved in N-glycosylation through its association with N-oligosaccharyl transferase.<ref>PMID:19717468</ref> [[http://www.uniprot.org/uniprot/CRBN_HUMAN CRBN_HUMAN]] Component of some DCX (DDB1-CUL4-X-box) E3 protein ligase complex, a complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins and is required for limb outgrowth and expression of the fibroblast growth factor FGF8. In the complex, may act as a substrate receptor. Regulates the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1.<ref>PMID:18414909</ref> <ref>PMID:20223979</ref>		[[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Magnesium transporter. May be involved in N-glycosylation through its association with N-oligosaccharyl transferase.<ref>PMID:19717468</ref> [[http://www.uniprot.org/uniprot/CRBN_HUMAN CRBN_HUMAN]] Component of some DCX (DDB1-CUL4-X-box) E3 protein ligase complex, a complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins and is required for limb outgrowth and expression of the fibroblast growth factor FGF8. In the complex, may act as a substrate receptor. Regulates the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1.<ref>PMID:18414909</ref> <ref>PMID:20223979</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	N-linked glycosylation of proteins in the endoplasmic reticulum (ER) is essential in eukaryotes and catalyzed by oligosaccharyl transferase (OST). Human OST is a hetero-oligomer of seven subunits. The subunit N33/Tusc3 is a tumor suppressor candidate, and defects in the subunit N33/Tusc3 are linked with nonsyndromic mental retardation. Here, we show that N33/Tusc3 possesses a membrane-anchored N-terminal thioredoxin domain located in the ER lumen that may form transient mixed disulfide complexes with OST substrates. X-ray structures of complexes between N33/Tusc3 and two different peptides as model substrates reveal a defined peptide-binding groove adjacent to the active site that can accommodate peptides in opposite orientations. Structural and biochemical data show that N33/Tusc3 prefers peptides bearing a hydrophobic residue two residues away from the cysteine forming the mixed disulfide with N33/Tusc3. Our results support a model in which N33/Tusc3 increases glycosylation efficiency for a subset of human glycoproteins by slowing glycoprotein folding.

-	~~==About this~~ Structure==	+	Structural basis of substrate specificity of human oligosaccharyl transferase subunit n33/tusc3 and its role in regulating protein N-glycosylation.,Mohorko E, Owen RL, Malojcic G, Brozzo MS, Aebi M, Glockshuber R Structure. 2014 Apr 8;22(4):590-601. doi: 10.1016/j.str.2014.02.013. Epub 2014, Mar 27. PMID:24685145<ref>PMID:24685145</ref>
-	~~[[4m91]] is a 2 chain structure~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.~~il/oca-bin/ocashort?id=4M91 OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-	<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
	[[Category: Aebi, M.]]		[[Category: Aebi, M.]]
	[[Category: Brozzo, M S.]]		[[Category: Brozzo, M S.]]

OCA at 09:34, 26 March 2014

OCA — Wed, 26 Mar 2014 09:34:59 GMT

←Older revision		Revision as of 09:34, 26 March 2014
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-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4m91\| PDB=4m91 \| SCENE= }}
		+	===crystal structure of hN33/Tusc3-peptide 1===

-	The entry ~~4m91~~ is ~~ON HOLD until Paper Publication~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/CRBN_HUMAN CRBN_HUMAN]] Autosomal recessive nonsyndromic intellectual deficit;Distal monosomy 3p. The disease is caused by mutations affecting the gene represented in this entry.

-	~~Authors~~: ~~Mohorko, E~~.~~, Owen, R~~.L.~~, Malojcic, G~~.~~, Brozzo, M~~.S., ~~Aebi, M~~., ~~Glockshuber, R~~.	+	==Function==
		+	[[http://www.uniprot.org/uniprot/TUSC3_HUMAN TUSC3_HUMAN]] Magnesium transporter. May be involved in N-glycosylation through its association with N-oligosaccharyl transferase.<ref>PMID:19717468</ref> [[http://www.uniprot.org/uniprot/CRBN_HUMAN CRBN_HUMAN]] Component of some DCX (DDB1-CUL4-X-box) E3 protein ligase complex, a complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins and is required for limb outgrowth and expression of the fibroblast growth factor FGF8. In the complex, may act as a substrate receptor. Regulates the assembly and neuronal surface expression of large-conductance calcium-activated potassium channels in brain regions involved in memory and learning via its interaction with KCNT1.<ref>PMID:18414909</ref> <ref>PMID:20223979</ref>

-	~~Description: crystal~~ structure ~~of hN33~~/~~Tusc3~~-~~peptide 1~~	+	==About this Structure==
		+	[[4m91]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M91 OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Aebi, M.]]
		+	[[Category: Brozzo, M S.]]
		+	[[Category: Glockshuber, R.]]
		+	[[Category: Malojcic, G.]]
		+	[[Category: Mohorko, E.]]
		+	[[Category: Owen, R L.]]
		+	[[Category: Endoplasmic reticulum]]
		+	[[Category: Formation of mixed disulfide]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Thioredoxin-like fold]]

OCA at 09:59, 4 September 2013

OCA — Wed, 04 Sep 2013 09:59:37 GMT

←Older revision		Revision as of 09:59, 4 September 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4m91 is ON HOLD	+	The entry 4m91 is ON HOLD until Paper Publication

	Authors: Mohorko, E., Owen, R.L., Malojcic, G., Brozzo, M.S., Aebi, M., Glockshuber, R.		Authors: Mohorko, E., Owen, R.L., Malojcic, G., Brozzo, M.S., Aebi, M., Glockshuber, R.

	Description: crystal structure of hN33/Tusc3-peptide 1		Description: crystal structure of hN33/Tusc3-peptide 1

OCA: Protected "4m91" [edit=sysop:move=sysop]

OCA — Wed, 21 Aug 2013 07:59:29 GMT

Protected "4m91" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:59, 21 August 2013

OCA: New page: '''Unreleased structure''' The entry 4m91 is ON HOLD Authors: Mohorko, E., Owen, R.L., Malojcic, G., Brozzo, M.S., Aebi, M., Glockshuber, R. Description: crystal structure of hN33/Tusc...

OCA — Wed, 21 Aug 2013 07:59:28 GMT

New page: '''Unreleased structure''' The entry 4m91 is ON HOLD Authors: Mohorko, E., Owen, R.L., Malojcic, G., Brozzo, M.S., Aebi, M., Glockshuber, R. Description: crystal structure of hN33/Tusc...

New page

'''Unreleased structure'''

The entry 4m91 is ON HOLD

Authors: Mohorko, E., Owen, R.L., Malojcic, G., Brozzo, M.S., Aebi, M., Glockshuber, R.

Description: crystal structure of hN33/Tusc3-peptide 1