4kxk - Revision history

OCA at 16:06, 20 September 2023

OCA — Wed, 20 Sep 2023 16:06:42 GMT

←Older revision		Revision as of 16:06, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4kxk]] is a 4 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=4KXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KXK FirstGlance]. <br>		<table><tr><td colspan='2'>[[4kxk]] is a 4 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=4KXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KXK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.9Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxk OCA], [https://pdbe.org/4kxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kxk RCSB], [https://www.ebi.ac.uk/pdbsum/4kxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kxk 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=4kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxk OCA], [https://pdbe.org/4kxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kxk RCSB], [https://www.ebi.ac.uk/pdbsum/4kxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kxk ProSAT]</span></td></tr>
	</table>		</table>

OCA at 09:20, 7 December 2022

OCA — Wed, 07 Dec 2022 09:20:13 GMT

←Older revision		Revision as of 09:20, 7 December 2022
Line 3:		Line 3:
	<StructureSection load='4kxk' size='340' side='right'caption='[[4kxk]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4kxk' size='340' side='right'caption='[[4kxk]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4kxk]] is a 4 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=4KXK OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4KXK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4kxk]] is a 4 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=4KXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KXK FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r9a\|3r9a]], [[4kyo\|4kyo]]</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=4kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxk OCA], [https://pdbe.org/4kxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kxk RCSB], [https://www.ebi.ac.uk/pdbsum/4kxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kxk ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AGXT, AGT1, SPAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PEX5, PXR1 ([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=4kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxk OCA], [~~http~~://pdbe.org/4kxk PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4kxk RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4kxk PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4kxk ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/~~SPYA_HUMAN SPYA_HUMAN~~]~~] Defects in AGXT are the cause of~~ hyperoxaluria ~~primary~~ type 1 ~~(HP1) [MIM:[http://omim~~.~~org/entry/259900 259900]]; also known as primary hyperoxaluria type I (PH1) and oxalosis I. HP1~~ is ~~a rare autosomal recessive inborn error of glyoxylate metabolism characterized~~ by ~~increased excretion of oxalate and glycolate, and~~ the ~~progressive accumulation of insoluble calcium oxalate~~ in the kidney and urinary tract.<ref>PMID:1703535</ref> <ref>PMID:2039493</ref> <ref>PMID:1349575</ref> <ref>PMID:1301173</ref> <ref>PMID:8101040</ref> <ref>PMID:9192270</ref> <ref>PMID:9604803</ref> <ref>PMID:10394939</ref> <ref>PMID:10453743</ref> <ref>PMID:10541294</ref> <ref>PMID:10862087</ref> <ref>PMID:10960483</ref> <ref>PMID:12559847</ref> <ref>PMID:12777626</ref> <ref>PMID:15253729</ref> <ref>PMID:15849466</ref> <ref>PMID:15961946</ref> <ref>PMID:15963748</ref> [[http://www.uniprot.org/uniprot/PEX5_HUMAN PEX5_HUMAN]] Defects in PEX5 are the cause of peroxisome biogenesis disorder 2A (PBD2A) [MIM:[http://omim.org/entry/214110 214110]]. A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and characterized clinically by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life.<ref>PMID:7719337</ref> Defects in PEX5 are the cause of peroxisome biogenesis disorder 2B (PBD2B) [MIM:[http://omim.org/entry/202370 202370]]. A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid.	+	[https://www.uniprot.org/uniprot/AGT1_HUMAN AGT1_HUMAN] Primary hyperoxaluria type 1. The disease is caused by variants affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~PEX5_HUMAN PEX5_HUMAN~~]~~] Binds~~ to the C-~~terminal PTS1~~-~~type tripeptide peroxisomal targeting signal~~ (~~SKL-type~~) ~~and plays an essential role in peroxisomal protein import~~.<ref>PMID:~~7719337~~</ref> <ref>PMID:~~7790377~~</ref> <ref>PMID:~~7706321~~</ref>	+	[https://www.uniprot.org/uniprot/AGT1_HUMAN AGT1_HUMAN] Peroxisomal aminotransferase that catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification (PubMed:10960483, PubMed:12777626, PubMed:24055001, PubMed:23229545, PubMed:26149463). Also catalyzes the transamination between L-serine and pyruvate and contributes to gluconeogenesis from the L-serine metabolism (PubMed:10347152).<ref>PMID:10347152</ref> <ref>PMID:10960483</ref> <ref>PMID:12777626</ref> <ref>PMID:23229545</ref> <ref>PMID:24055001</ref> <ref>PMID:26149463</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 29:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Fodor, K]]	+	[[Category: Fodor K]]
-	[[Category: Lou, Y]]	+	[[Category: Lou Y]]
-	[[Category: Wilmanns, M]]	+	[[Category: Wilmanns M]]
-	~~[[Category: Aminotransferase]]~~	+
-	~~[[Category: Peroxisomal import]]~~	+
-	~~[[Category: Peroxisome]]~~	+
-	~~[[Category: Primary hyperoxaluria]]~~	+
-	~~[[Category: Pyruvate]]~~	+
-	~~[[Category: Tpr-domain]]~~	+
-	~~[[Category: Transferase-transport protein complex]]~~	+
-	~~[[Category: Transport~~]]	+

OCA at 09:39, 3 April 2019

OCA — Wed, 03 Apr 2019 09:39:02 GMT

←Older revision		Revision as of 09:39, 3 April 2019
Line 1:		Line 1:

	==Alanine-glyoxylate aminotransferase variant K390A/K391A in complex with the TPR domain of human Pex5p==		==Alanine-glyoxylate aminotransferase variant K390A/K391A in complex with the TPR domain of human Pex5p==
-	<StructureSection load='4kxk' size='340' side='right' caption='[[4kxk]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='4kxk' size='340' side='right'caption='[[4kxk]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4kxk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KXK FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4kxk]] is a 4 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=4KXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KXK FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r9a\|3r9a]], [[4kyo\|4kyo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r9a\|3r9a]], [[4kyo\|4kyo]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">AGXT, AGT1, SPAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PEX5, PXR1 ([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=4kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxk OCA], [http://pdbe.org/4kxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kxk RCSB], [http://www.ebi.ac.uk/pdbsum/4kxk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kxk ProSAT]</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=4kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxk OCA], [http://pdbe.org/4kxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kxk RCSB], [http://www.ebi.ac.uk/pdbsum/4kxk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kxk ProSAT]</span></td></tr>
	</table>		</table>
Line 23:		Line 24:

	==See Also==		==See Also==
-	*[[Aminotransferase\|Aminotransferase]]	+	*[[Aminotransferase 3D structures\|Aminotransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Fodor, K]]		[[Category: Fodor, K]]
	[[Category: Lou, Y]]		[[Category: Lou, Y]]

OCA at 11:22, 11 August 2016

OCA — Thu, 11 Aug 2016 11:22:18 GMT

←Older revision		Revision as of 11:22, 11 August 2016
Line 1:		Line 1:
		+
	==Alanine-glyoxylate aminotransferase variant K390A/K391A in complex with the TPR domain of human Pex5p==		==Alanine-glyoxylate aminotransferase variant K390A/K391A in complex with the TPR domain of human Pex5p==
	<StructureSection load='4kxk' size='340' side='right' caption='[[4kxk]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4kxk' size='340' side='right' caption='[[4kxk]], [[Resolution\|resolution]] 2.90Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r9a\|3r9a]], [[4kyo\|4kyo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r9a\|3r9a]], [[4kyo\|4kyo]]</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=4kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kxk RCSB], [http://www.ebi.ac.uk/pdbsum/4kxk 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=4kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxk OCA], [http://pdbe.org/4kxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kxk RCSB], [http://www.ebi.ac.uk/pdbsum/4kxk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kxk 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 4kxk" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminotransferase\|Aminotransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:45, 19 November 2014

OCA — Wed, 19 Nov 2014 12:45:02 GMT

←Older revision		Revision as of 12:45, 19 November 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Alanine-glyoxylate aminotransferase variant K390A/K391A in complex with the TPR domain of human Pex5p==
		+	<StructureSection load='4kxk' size='340' side='right' caption='[[4kxk]], [[Resolution\|resolution]] 2.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4kxk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KXK FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3r9a\|3r9a]], [[4kyo\|4kyo]]</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=4kxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4kxk RCSB], [http://www.ebi.ac.uk/pdbsum/4kxk PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/SPYA_HUMAN SPYA_HUMAN]] Defects in AGXT are the cause of hyperoxaluria primary type 1 (HP1) [MIM:[http://omim.org/entry/259900 259900]]; also known as primary hyperoxaluria type I (PH1) and oxalosis I. HP1 is a rare autosomal recessive inborn error of glyoxylate metabolism characterized by increased excretion of oxalate and glycolate, and the progressive accumulation of insoluble calcium oxalate in the kidney and urinary tract.<ref>PMID:1703535</ref> <ref>PMID:2039493</ref> <ref>PMID:1349575</ref> <ref>PMID:1301173</ref> <ref>PMID:8101040</ref> <ref>PMID:9192270</ref> <ref>PMID:9604803</ref> <ref>PMID:10394939</ref> <ref>PMID:10453743</ref> <ref>PMID:10541294</ref> <ref>PMID:10862087</ref> <ref>PMID:10960483</ref> <ref>PMID:12559847</ref> <ref>PMID:12777626</ref> <ref>PMID:15253729</ref> <ref>PMID:15849466</ref> <ref>PMID:15961946</ref> <ref>PMID:15963748</ref> [[http://www.uniprot.org/uniprot/PEX5_HUMAN PEX5_HUMAN]] Defects in PEX5 are the cause of peroxisome biogenesis disorder 2A (PBD2A) [MIM:[http://omim.org/entry/214110 214110]]. A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and characterized clinically by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life.<ref>PMID:7719337</ref> Defects in PEX5 are the cause of peroxisome biogenesis disorder 2B (PBD2B) [MIM:[http://omim.org/entry/202370 202370]]. A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PEX5_HUMAN PEX5_HUMAN]] Binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import.<ref>PMID:7719337</ref> <ref>PMID:7790377</ref> <ref>PMID:7706321</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Peroxisomes entirely rely on the import of their proteome across the peroxisomal membrane. Recognition efficiencies of peroxisomal proteins vary by more than 1000-fold but the molecular rationale behind their subsequent differential import and sorting has remained enigmatic. Using the protein cargo alanine-glyoxylate aminotransferase as a model, we have discovered an unexpected increase from 34% to 80% in peroxisomal import efficiency of a single-residue mutant. By high-resolution structural analysis, we found that it is the recognition receptor PEX5 that adapts its conformation for high-affinity binding rather than the cargo protein signal motif as previously thought. During receptor recognition, the binding cavity of the receptor shrinks to one third of its original volume. This process is impeded in the wild-type protein cargo because of a bulky side chain within the recognition motif, which blocks contraction of the PEX5 binding cavity. Our data provide a new insight on direct protein import efficiency by removal rather than addition of an apparent specific sequence signature that is generally applicable to peroxisomal matrix proteins and to other receptor recognition processes.

-	~~The entry 4kxk is ON HOLD until Paper Publication~~	+	Ligand-induced compaction of the PEX5 receptor-binding cavity impacts protein import efficiency into peroxisomes.,Fodor K, Wolf J, Reglinski K, Passon DM, Lou Y, Schliebs W, Erdmann R, Wilmanns M Traffic. 2014 Nov 5. doi: 10.1111/tra.12238. PMID:25369882<ref>PMID:25369882</ref>

-	~~Authors~~: Fodor, K., Lou, Y., Wilmanns, M.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Alanine~~-~~glyoxylate aminotransferase variant K390A/K391A in complex with the TPR~~ domain ~~of human Pex5p~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Fodor, K]]
		+	[[Category: Lou, Y]]
		+	[[Category: Wilmanns, M]]
		+	[[Category: Aminotransferase]]
		+	[[Category: Peroxisomal import]]
		+	[[Category: Peroxisome]]
		+	[[Category: Primary hyperoxaluria]]
		+	[[Category: Pyruvate]]
		+	[[Category: Tpr-domain]]
		+	[[Category: Transferase-transport protein complex]]
		+	[[Category: Transport]]

OCA at 08:55, 30 June 2013

OCA — Sun, 30 Jun 2013 08:55:56 GMT

←Older revision		Revision as of 08:55, 30 June 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Fodor, K., Lou, Y., Wilmanns, M.		Authors: Fodor, K., Lou, Y., Wilmanns, M.

	Description: Alanine-glyoxylate aminotransferase variant K390A/K391A in complex with the TPR domain of human Pex5p		Description: Alanine-glyoxylate aminotransferase variant K390A/K391A in complex with the TPR domain of human Pex5p

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

OCA — Wed, 19 Jun 2013 12:11:28 GMT

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

←Older revision

Revision as of 12:11, 19 June 2013

OCA: New page: '''Unreleased structure''' The entry 4kxk is ON HOLD Authors: Fodor, K., Lou, Y., Wilmanns, M. Description: Alanine-glyoxylate aminotransferase variant K390A/K391A in complex with the ...

OCA — Wed, 19 Jun 2013 12:11:28 GMT

New page: '''Unreleased structure''' The entry 4kxk is ON HOLD Authors: Fodor, K., Lou, Y., Wilmanns, M. Description: Alanine-glyoxylate aminotransferase variant K390A/K391A in complex with the ...

New page

'''Unreleased structure'''

The entry 4kxk is ON HOLD

Authors: Fodor, K., Lou, Y., Wilmanns, M.

Description: Alanine-glyoxylate aminotransferase variant K390A/K391A in complex with the TPR domain of human Pex5p