4gg2 - Revision history

OCA at 15:45, 14 March 2024

OCA — Thu, 14 Mar 2024 15:45:54 GMT

←Older revision		Revision as of 15:45, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4gg2]] 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=4GG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GG2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4gg2]] 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=4GG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GG2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.21Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4gg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gg2 OCA], [https://pdbe.org/4gg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gg2 RCSB], [https://www.ebi.ac.uk/pdbsum/4gg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gg2 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=4gg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gg2 OCA], [https://pdbe.org/4gg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gg2 RCSB], [https://www.ebi.ac.uk/pdbsum/4gg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gg2 ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>		[https://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The enzyme gamma-glutamyl transpeptidase 1 (GGT1) is a conserved member of the Nterminal nucleophile (Ntn)-hydroylase family that cleaves the gamma-glutamyl bond of glutathione and other gamma-glutamyl compounds. In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status. Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer. The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model. The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs. We report the high-resolution (1.67 A) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT. Comparisons of the active site architecture of hGGT1 to those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme. Compared to several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site. The hGGT1 structure also revealed tightly bound chlorides near the catalytic residue that may contribute to catalytic activity. These are absent in the bacterial GGTs. These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.
-
-	Novel insights into eukaryotic gamma-glutamyl transpeptidase 1 from the crystal structure of the glutamate-bound human enzyme.,West MB, Chen Y, Wickham S, Heroux A, Cahill K, Hanigan MH, Mooers BH J Biol Chem. 2013 Sep 18. PMID:24047895<ref>PMID:24047895</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4gg2" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:55, 26 October 2022

OCA — Wed, 26 Oct 2022 06:55:04 GMT

←Older revision		Revision as of 06:55, 26 October 2022
Line 1:		Line 1:

	==The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1==		==The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1==
-	<StructureSection load='4gg2' size='340' side='right' caption='[[4gg2]], [[Resolution\|resolution]] 2.21Å' scene=''>	+	<StructureSection load='4gg2' size='340' side='right'caption='[[4gg2]], [[Resolution\|resolution]] 2.21Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gg2]] 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=4GG2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GG2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gg2]] 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=4GG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GG2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dgx\|4dgx]]</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=4gg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gg2 OCA], [https://pdbe.org/4gg2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gg2 RCSB], [https://www.ebi.ac.uk/pdbsum/4gg2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gg2 ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GGT, GGT1, hGGT1 ([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=4gg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gg2 OCA], [~~http~~://pdbe.org/4gg2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gg2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gg2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gg2 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>	+	[https://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: Cahill, K]]	+	[[Category: Large Structures]]
-	[[Category: Chen, Y]]	+	[[Category: Cahill K]]
-	[[Category: Hanigan~~, M H~~]]	+	[[Category: Chen Y]]
-	[[Category: Heroux, A]]	+	[[Category: Hanigan MH]]
-	[[Category: Mooers~~, B H.M~~]]	+	[[Category: Heroux A]]
-	[[Category: West~~, M B~~]]	+	[[Category: Mooers BHM]]
-	[[Category: Wickham, S]]	+	[[Category: West MB]]
-	~~[[Category: Exterior cell surface]]~~	+	[[Category: Wickham S]]
-	~~[[Category: Glutathionine metabolism]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: N-glycosylation]]~~	+
-	~~[[Category: Ntn-hydrolyase~~]]	+

OCA at 12:29, 5 August 2016

OCA — Fri, 05 Aug 2016 12:29:58 GMT

←Older revision		Revision as of 12:29, 5 August 2016
Line 1:		Line 1:
		+
	==The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1==		==The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1==
	<StructureSection load='4gg2' size='340' side='right' caption='[[4gg2]], [[Resolution\|resolution]] 2.21Å' scene=''>		<StructureSection load='4gg2' size='340' side='right' caption='[[4gg2]], [[Resolution\|resolution]] 2.21Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dgx\|4dgx]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dgx\|4dgx]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GGT, GGT1, hGGT1 ([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">GGT, GGT1, hGGT1 ([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=4gg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gg2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gg2 RCSB], [http://www.ebi.ac.uk/pdbsum/4gg2 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=4gg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gg2 OCA], [http://pdbe.org/4gg2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gg2 RCSB], [http://www.ebi.ac.uk/pdbsum/4gg2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gg2 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	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 4gg2" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:31, 21 December 2014

OCA — Sun, 21 Dec 2014 18:31:14 GMT

←Older revision		Revision as of 18:31, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4gg2\| PDB=4gg2 \| SCENE= }}~~	+	==The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1==
-	===The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1===	+	<StructureSection load='4gg2' size='340' side='right' caption='[[4gg2]], [[Resolution\|resolution]] 2.21Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24047895}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4gg2]] 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=4GG2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GG2 FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dgx\|4dgx]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">GGT, GGT1, hGGT1 ([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=4gg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gg2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gg2 RCSB], [http://www.ebi.ac.uk/pdbsum/4gg2 PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.		[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>		[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The enzyme gamma-glutamyl transpeptidase 1 (GGT1) is a conserved member of the Nterminal nucleophile (Ntn)-hydroylase family that cleaves the gamma-glutamyl bond of glutathione and other gamma-glutamyl compounds. In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status. Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer. The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model. The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs. We report the high-resolution (1.67 A) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT. Comparisons of the active site architecture of hGGT1 to those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme. Compared to several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site. The hGGT1 structure also revealed tightly bound chlorides near the catalytic residue that may contribute to catalytic activity. These are absent in the bacterial GGTs. These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.

-	~~==About this Structure==~~	+	Novel insights into eukaryotic gamma-glutamyl transpeptidase 1 from the crystal structure of the glutamate-bound human enzyme.,West MB, Chen Y, Wickham S, Heroux A, Cahill K, Hanigan MH, Mooers BH J Biol Chem. 2013 Sep 18. PMID:24047895<ref>PMID:24047895</ref>
-	~~[[4gg2]] 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=4GG2 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024047895</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Cahill, K.]]	+	[[Category: Cahill, K]]
-	[[Category: Chen, Y.]]	+	[[Category: Chen, Y]]
-	[[Category: Hanigan, M H.]]	+	[[Category: Hanigan, M H]]
-	[[Category: Heroux, A.]]	+	[[Category: Heroux, A]]
-	[[Category: Mooers, B H.M.]]	+	[[Category: Mooers, B H.M]]
-	[[Category: West, M B.]]	+	[[Category: West, M B]]
-	[[Category: Wickham, S.]]	+	[[Category: Wickham, S]]
	[[Category: Exterior cell surface]]		[[Category: Exterior cell surface]]
	[[Category: Glutathionine metabolism]]		[[Category: Glutathionine metabolism]]

OCA at 08:46, 27 November 2013

OCA — Wed, 27 Nov 2013 08:46:29 GMT

←Older revision		Revision as of 08:46, 27 November 2013
Line 10:		Line 10:

	==About this Structure==		==About this Structure==
-	[[4gg2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Zasmidium_angulare Zasmidium angulare~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GG2 OCA].	+	[[4gg2]] 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=4GG2 OCA].

	==Reference==		==Reference==
	<ref group="xtra">PMID:024047895</ref><references group="xtra"/><references/>		<ref group="xtra">PMID:024047895</ref><references group="xtra"/><references/>
-	[[Category: ~~Homo sapiens]]~~	+	[[Category: Human]]
-	~~[[Category: Zasmidium angulare~~]]	+
	[[Category: Cahill, K.]]		[[Category: Cahill, K.]]
	[[Category: Chen, Y.]]		[[Category: Chen, Y.]]

OCA at 06:51, 16 October 2013

OCA — Wed, 16 Oct 2013 06:51:53 GMT

←Older revision		Revision as of 06:51, 16 October 2013
Line 1:		Line 1:
	{{STRUCTURE_4gg2\| PDB=4gg2 \| SCENE= }}		{{STRUCTURE_4gg2\| PDB=4gg2 \| SCENE= }}
	===The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1===		===The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1===
		+	{{ABSTRACT_PUBMED_24047895}}

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

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024047895</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Zasmidium angulare]]		[[Category: Zasmidium angulare]]

OCA at 08:16, 29 September 2013

OCA — Sun, 29 Sep 2013 08:16:47 GMT

←Older revision		Revision as of 08:16, 29 September 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4gg2\| PDB=4gg2 \| SCENE= }}
		+	===The crystal structure of glutamate-bound human gamma-glutamyltranspeptidase 1===

-	The ~~entry 4gg2~~ is ~~ON HOLD until Sep 30 2014~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Gamma-glutamyl transpeptidase deficiency. The disease is caused by mutations affecting the gene represented in this entry.

-	~~Authors~~: ~~West, M~~.B., ~~Chen, Y~~.~~, Wickham, S~~.~~, Heroux, A~~., ~~Cahill, K~~.~~, Hanigan, M.H., Mooers, B.H.M~~.	+	==Function==
		+	[[http://www.uniprot.org/uniprot/GGT1_HUMAN GGT1_HUMAN]] Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.<ref>PMID:7689219</ref> <ref>PMID:20622017</ref>

-	~~Description: The crystal~~ structure ~~of glutamate~~-~~bound human~~-~~glutamyltranspeptidase 1~~	+	==About this Structure==
		+	[[4gg2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Zasmidium_angulare Zasmidium angulare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GG2 OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Zasmidium angulare]]
		+	[[Category: Cahill, K.]]
		+	[[Category: Chen, Y.]]
		+	[[Category: Hanigan, M H.]]
		+	[[Category: Heroux, A.]]
		+	[[Category: Mooers, B H.M.]]
		+	[[Category: West, M B.]]
		+	[[Category: Wickham, S.]]
		+	[[Category: Exterior cell surface]]
		+	[[Category: Glutathionine metabolism]]
		+	[[Category: Hydrolase]]
		+	[[Category: N-glycosylation]]
		+	[[Category: Ntn-hydrolyase]]

OCA at 09:33, 4 September 2013

OCA — Wed, 04 Sep 2013 09:33:09 GMT

←Older revision		Revision as of 09:33, 4 September 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gg2 is ON HOLD until ~~Paper Publication~~	+	The entry 4gg2 is ON HOLD until Sep 30 2014

	Authors: West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H.M.		Authors: West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H.M.

	Description: The crystal structure of glutamate-bound human-glutamyltranspeptidase 1		Description: The crystal structure of glutamate-bound human-glutamyltranspeptidase 1

OCA at 04:41, 18 July 2013

OCA — Thu, 18 Jul 2013 04:41:58 GMT

←Older revision		Revision as of 04:41, 18 July 2013
Line 3:		Line 3:
	The entry 4gg2 is ON HOLD until Paper Publication		The entry 4gg2 is ON HOLD until Paper Publication

-	Authors: West, MB, Chen, Y, Wickham, S, Heroux, A, Cahill, K, Hanigan, MH, Mooers, ~~BHM~~	+	Authors: West, M.B., Chen, Y., Wickham, S., Heroux, A., Cahill, K., Hanigan, M.H., Mooers, B.H.M.

	Description: The crystal structure of glutamate-bound human-glutamyltranspeptidase 1		Description: The crystal structure of glutamate-bound human-glutamyltranspeptidase 1

OCA at 13:58, 28 November 2012

OCA — Wed, 28 Nov 2012 13:58:41 GMT

←Older revision		Revision as of 13:58, 28 November 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gg2 is ON HOLD	+	The entry 4gg2 is ON HOLD until Paper Publication

	Authors: West, MB, Chen, Y, Wickham, S, Heroux, A, Cahill, K, Hanigan, MH, Mooers, BHM		Authors: West, MB, Chen, Y, Wickham, S, Heroux, A, Cahill, K, Hanigan, MH, Mooers, BHM

	Description: The crystal structure of glutamate-bound human-glutamyltranspeptidase 1		Description: The crystal structure of glutamate-bound human-glutamyltranspeptidase 1