4m92 - Revision history

OCA at 16:34, 20 September 2023

OCA — Wed, 20 Sep 2023 16:34:20 GMT

←Older revision		Revision as of 16:34, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4m92]] 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=4M92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M92 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4m92]] 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=4M92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M92 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=4m92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m92 OCA], [https://pdbe.org/4m92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m92 RCSB], [https://www.ebi.ac.uk/pdbsum/4m92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m92 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]] 1.6Å</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=4m92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m92 OCA], [https://pdbe.org/4m92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m92 RCSB], [https://www.ebi.ac.uk/pdbsum/4m92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m92 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 11:03, 21 December 2022

OCA — Wed, 21 Dec 2022 11:03:51 GMT

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

	==Crystal structure of hN33/Tusc3-peptide 2==		==Crystal structure of hN33/Tusc3-peptide 2==
-	<StructureSection load='4m92' size='340' side='right' caption='[[4m92]], [[Resolution\|resolution]] 1.60Å' scene=''>	+	<StructureSection load='4m92' size='340' side='right'caption='[[4m92]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4m92]] 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=4M92 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4M92 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4m92]] 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=4M92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M92 FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m91\|4m91]]</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=4m92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m92 OCA], [https://pdbe.org/4m92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m92 RCSB], [https://www.ebi.ac.uk/pdbsum/4m92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m92 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]), IL1RAPL1, OPHN4 ([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=4m92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m92 OCA], [~~http~~://pdbe.org/4m92 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4m92 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4m92 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4m92 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/IRPL1_HUMAN IRPL1_HUMAN]] Defects in IL1RAPL1 are the cause of mental retardation X-linked type 21 (MRX21) [MIM:[http://omim.org/entry/300143 300143]]. Mental retardation is a mental disorder characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs.<ref>PMID:10757639</ref> <ref>PMID:16470793</ref>	+	[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/IRPL1_HUMAN IRPL1_HUMAN]] May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in presynaptic and postsynaptic differentiation and dendritic spine formation in neurons.<ref>PMID:12783849</ref> <ref>PMID:15123616</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: Oxidoreductase]]~~	+	[[Category: Owen RL]]
-	~~[[Category: Redox-active protein]]~~	+
-	~~[[Category: Thiol/disulfide exchange reaction]]~~	+
-	~~[[Category: Thiol/disulfide oxidoreductase]]~~	+
-	~~[[Category: Thioredoxin-like fold~~]]	+

OCA at 20:17, 11 August 2016

OCA — Thu, 11 Aug 2016 20:17:07 GMT

←Older revision		Revision as of 20:17, 11 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of hN33/Tusc3-peptide 2==		==Crystal structure of hN33/Tusc3-peptide 2==
	<StructureSection load='4m92' size='340' side='right' caption='[[4m92]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='4m92' size='340' side='right' caption='[[4m92]], [[Resolution\|resolution]] 1.60Å' 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]], [[4m91\|4m91]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m91\|4m91]]</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]), IL1RAPL1, OPHN4 ([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]), IL1RAPL1, OPHN4 ([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=4m92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m92 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m92 RCSB], [http://www.ebi.ac.uk/pdbsum/4m92 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=4m92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m92 OCA], [http://pdbe.org/4m92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m92 RCSB], [http://www.ebi.ac.uk/pdbsum/4m92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m92 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 4m92" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:03, 5 January 2015

OCA — Mon, 05 Jan 2015 09:03:03 GMT

←Older revision		Revision as of 09:03, 5 January 2015
Line 2:		Line 2:
	<StructureSection load='4m92' size='340' side='right' caption='[[4m92]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='4m92' size='340' side='right' caption='[[4m92]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4m92]] 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=4M92 OCA]. <br>	+	<table><tr><td colspan='2'>[[4m92]] 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=4M92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M92 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m91\|4m91]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m91\|4m91]]</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]), IL1RAPL1, OPHN4 ([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]), IL1RAPL1, OPHN4 ([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=4m92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m92 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m92 RCSB], [http://www.ebi.ac.uk/pdbsum/4m92 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=4m92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m92 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m92 RCSB], [http://www.ebi.ac.uk/pdbsum/4m92 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/IRPL1_HUMAN IRPL1_HUMAN]] Defects in IL1RAPL1 are the cause of mental retardation X-linked type 21 (MRX21) [MIM:[http://omim.org/entry/300143 300143]]. Mental retardation is a mental disorder characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs.<ref>PMID:10757639</ref> <ref>PMID:16470793</ref>		[[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/IRPL1_HUMAN IRPL1_HUMAN]] Defects in IL1RAPL1 are the cause of mental retardation X-linked type 21 (MRX21) [MIM:[http://omim.org/entry/300143 300143]]. Mental retardation is a mental disorder characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs.<ref>PMID:10757639</ref> <ref>PMID:16470793</ref>
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: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Redox-active protein]]		[[Category: Redox-active protein]]

OCA at 06:45, 7 May 2014

OCA — Wed, 07 May 2014 06:45:04 GMT

←Older revision		Revision as of 06:45, 7 May 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4m92\| PDB~~=4m92 \| ~~SCENE~~= }}	+	==Crystal structure of hN33/Tusc3-peptide 2==
-	===~~Crystal~~ structure ~~of hN33~~/~~Tusc3~~-~~peptide~~ 2===	+	<StructureSection load='4m92' size='340' side='right' caption='[[4m92]], [[Resolution\|resolution]] 1.60Å' scene=''>
-		+	== Structural highlights ==
-	==Disease==	+	<table><tr><td colspan='2'>[[4m92]] 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=4M92 OCA]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4m8g\|4m8g]], [[4m90\|4m90]], [[4m91\|4m91]]</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]), IL1RAPL1, OPHN4 ([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=4m92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m92 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m92 RCSB], [http://www.ebi.ac.uk/pdbsum/4m92 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/IRPL1_HUMAN IRPL1_HUMAN]] Defects in IL1RAPL1 are the cause of mental retardation X-linked type 21 (MRX21) [MIM:[http://omim.org/entry/300143 300143]]. Mental retardation is a mental disorder characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs.<ref>PMID:10757639</ref> <ref>PMID:16470793</ref>		[[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/IRPL1_HUMAN IRPL1_HUMAN]] Defects in IL1RAPL1 are the cause of mental retardation X-linked type 21 (MRX21) [MIM:[http://omim.org/entry/300143 300143]]. Mental retardation is a mental disorder characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs.<ref>PMID:10757639</ref> <ref>PMID:16470793</ref>
-		+	== 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/IRPL1_HUMAN IRPL1_HUMAN]] May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in presynaptic and postsynaptic differentiation and dendritic spine formation in neurons.<ref>PMID:12783849</ref> <ref>PMID:15123616</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/IRPL1_HUMAN IRPL1_HUMAN]] May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in presynaptic and postsynaptic differentiation and dendritic spine formation in neurons.<ref>PMID:12783849</ref> <ref>PMID:15123616</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>
-	~~[[4m92]] is a 2 chain structure~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.ac.~~il/oca-bin/ocashort?id=4M92 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 09:35, 26 March 2014

OCA — Wed, 26 Mar 2014 09:35:04 GMT

←Older revision		Revision as of 09:35, 26 March 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4m92\| PDB=4m92 \| SCENE= }}
		+	===Crystal structure of hN33/Tusc3-peptide 2===

-	The entry ~~4m92~~ 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/IRPL1_HUMAN IRPL1_HUMAN]] Defects in IL1RAPL1 are the cause of mental retardation X-linked type 21 (MRX21) [MIM:[http://omim.org/entry/300143 300143]]. Mental retardation is a mental disorder characterized by significantly sub-average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Non-syndromic mental retardation patients do not manifest other clinical signs.<ref>PMID:10757639</ref> <ref>PMID:16470793</ref>

-	~~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/IRPL1_HUMAN IRPL1_HUMAN]] May regulate secretion and presynaptic differentiation through inhibition of the activity of N-type voltage-gated calcium channel. May activate the MAP kinase JNK. Plays a role in presynaptic and postsynaptic differentiation and dendritic spine formation in neurons.<ref>PMID:12783849</ref> <ref>PMID:15123616</ref>

-	~~Description: Crystal~~ structure ~~of hN33~~/~~Tusc3~~-~~peptide 2~~	+	==About this Structure==
		+	[[4m92]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M92 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: Oxidoreductase]]
		+	[[Category: Redox-active protein]]
		+	[[Category: Thiol/disulfide exchange reaction]]
		+	[[Category: Thiol/disulfide oxidoreductase]]
		+	[[Category: Thioredoxin-like fold]]

OCA at 09:59, 4 September 2013

OCA — Wed, 04 Sep 2013 09:59:40 GMT

←Older revision		Revision as of 09:59, 4 September 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4m92 is ON HOLD	+	The entry 4m92 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 2	+	Description: Crystal structure of hN33/Tusc3-peptide 2

OCA: Protected "4m92" [edit=sysop:move=sysop]

OCA — Wed, 21 Aug 2013 07:59:31 GMT

Protected "4m92" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:59, 21 August 2013

OCA: New page: '''Unreleased structure''' The entry 4m92 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 07:59:31 GMT

New page: '''Unreleased structure''' The entry 4m92 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 4m92 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 2