5lg6 - Revision history

OCA at 08:59, 11 October 2023

2023-10-11T08:59:05Z

←Older revision		Revision as of 08:59, 11 October 2023
Line 3:		Line 3:
	<StructureSection load='5lg6' size='340' side='right'caption='[[5lg6]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='5lg6' size='340' side='right'caption='[[5lg6]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lg6]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Pig Pig~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LG6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5LG6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lg6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LG6 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NAG:N~~-~~ACETYL-D-GLUCOSAMINE'>NAG</scene>~~, ~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.5Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td><~~td class="sblockDat">ANPEP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</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=5lg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lg6 OCA], [https://pdbe.org/5lg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lg6 RCSB], [https://www.ebi.ac.uk/pdbsum/5lg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lg6 ProSAT]</span></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2]~~ </~~span~~></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5lg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lg6 OCA], [~~http~~://pdbe.org/5lg6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5lg6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5lg6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5lg6 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/AMPN_PIG AMPN_PIG]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner.<ref>PMID:7913510</ref> <ref>PMID:1350661</ref> <ref>PMID:7911642</ref> <ref>PMID:8985407</ref> <ref>PMID:9634079</ref>	+	[https://www.uniprot.org/uniprot/AMPN_PIG AMPN_PIG] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner.<ref>PMID:7913510</ref> <ref>PMID:1350661</ref> <ref>PMID:7911642</ref> <ref>PMID:8985407</ref> <ref>PMID:9634079</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 29:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Membrane alanyl aminopeptidase]]~~	+	[[Category: Sus scrofa]]
-	~~[[Category: Pig~~]]	+	[[Category: Casasnovas JM]]
-	[[Category: Casasnovas~~, J M~~]]	+	[[Category: Mudgal G]]
-	[[Category: Mudgal, G]]	+	[[Category: Reguera J]]
-	[[Category: Reguera, J]]	+	[[Category: Santiago C]]
-	[[Category: Santiago, C]]	+
-	~~[[Category: Cd13]]~~	+
-	~~[[Category: Coronavirus]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Papn]]~~	+
-	~~[[Category: Porcine aminopeptidase n~~]]	+

OCA at 10:36, 12 August 2020

2020-08-12T10:36:01Z

←Older revision		Revision as of 10:36, 12 August 2020
Line 1:		Line 1:

	==Structure of the deglycosylated porcine aminopeptidase N ectodomain==		==Structure of the deglycosylated porcine aminopeptidase N ectodomain==
-	<StructureSection load='5lg6' size='340' side='right' caption='[[5lg6]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='5lg6' size='340' side='right'caption='[[5lg6]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lg6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LG6 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5LG6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lg6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LG6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LG6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANPEP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </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=5lg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lg6 OCA], [http://pdbe.org/5lg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lg6 RCSB], [http://www.ebi.ac.uk/pdbsum/5lg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lg6 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lg6 OCA], [http://pdbe.org/5lg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lg6 RCSB], [http://www.ebi.ac.uk/pdbsum/5lg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lg6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5lg6" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5lg6" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Membrane alanyl aminopeptidase]]		[[Category: Membrane alanyl aminopeptidase]]
		+	[[Category: Pig]]
	[[Category: Casasnovas, J M]]		[[Category: Casasnovas, J M]]
	[[Category: Mudgal, G]]		[[Category: Mudgal, G]]

OCA at 06:02, 19 April 2017

2017-04-19T06:02:39Z

←Older revision		Revision as of 06:02, 19 April 2017
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/AMPN_PIG AMPN_PIG]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner.<ref>PMID:7913510</ref> <ref>PMID:1350661</ref> <ref>PMID:7911642</ref> <ref>PMID:8985407</ref> <ref>PMID:9634079</ref>		[[http://www.uniprot.org/uniprot/AMPN_PIG AMPN_PIG]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner.<ref>PMID:7913510</ref> <ref>PMID:1350661</ref> <ref>PMID:7911642</ref> <ref>PMID:8985407</ref> <ref>PMID:9634079</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Cell surface aminopeptidase N (APN) is a membrane-bound ectoenzyme that hydrolyzes proteins and peptides and regulates numerous cell functions. APN participates in tumor cell expansion and motility, and is a target for cancer therapies. Small drugs that bind to the APN active site inhibit catalysis and suppress tumor growth. APN is also a major cell entry receptor for coronavirus, which binds to a region distant from the active site. Three crystal structures that we determined of human and pig APN ectodomains defined the dynamic conformation of the protein. These structures offered snapshots of closed, intermediate and open APN, which represent distinct functional states. Coronavirus envelope proteins specifically recognized the open APN form, prevented ectodomain progression to the closed form and substrate hydrolysis. In addition, drugs that bind the active site inhibited both coronavirus binding to cell surface APN and infection; the drugs probably hindered APN transition to the virus-specific open form. We conclude that allosteric inhibition of APN functions occurs by ligand suppression of ectodomain motions necessary for catalysis and virus cell entry, as validated by locking APN with disulfides. Blocking APN dynamics can thus be a valuable approach to development of drugs that target this ectoenzyme.
		+
		+	Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection.,Santiago C, Mudgal G, Reguera J, Recacha R, Albrecht S, Enjuanes L, Casasnovas JM Sci Rep. 2017 Apr 10;7:46045. doi: 10.1038/srep46045. PMID:28393915<ref>PMID:28393915</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5lg6" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:44, 12 April 2017

2017-04-12T11:44:31Z

←Older revision		Revision as of 11:44, 12 April 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5lg6 is ~~ON HOLD~~	+	==Structure of the deglycosylated porcine aminopeptidase N ectodomain==
-		+	<StructureSection load='5lg6' size='340' side='right' caption='[[5lg6]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~Authors~~: ~~Santiago~~, C., ~~Reguera~~, J., ~~Mudgal~~, G., ~~Casasnovas, J~~.M.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5lg6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LG6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LG6 FirstGlance]. <br>
-	~~Description~~: ~~Structure~~ of the ~~deglycosylated~~ porcine aminopeptidase ~~N ectodomain~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] </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=5lg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lg6 OCA], [http://pdbe.org/5lg6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lg6 RCSB], [http://www.ebi.ac.uk/pdbsum/5lg6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lg6 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AMPN_PIG AMPN_PIG]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity). It is able to degrade Leu-enkephalin and Met-enkephalin but not cholecystokinin CCK8, neuromedin C (GRP-10), somatostatin-14, substance P and vasoactive intestinal peptide. In case of porcine transmissible gastroenteritis coronavirus (TGEV) and porcine respiratory coronavirus (PRCoV) infections, serves as a receptor for TGEV and PRCoV spike glycoprotein in a species-specific manner.<ref>PMID:7913510</ref> <ref>PMID:1350661</ref> <ref>PMID:7911642</ref> <ref>PMID:8985407</ref> <ref>PMID:9634079</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Membrane alanyl aminopeptidase]]
		+	[[Category: Casasnovas, J M]]
		+	[[Category: Mudgal, G]]
	[[Category: Reguera, J]]		[[Category: Reguera, J]]
-	[[Category: Casasnovas, J.M]]
-	[[Category: Mudgal, G]]
	[[Category: Santiago, C]]		[[Category: Santiago, C]]
		+	[[Category: Cd13]]
		+	[[Category: Coronavirus]]
		+	[[Category: Hydrolase]]
		+	[[Category: Papn]]
		+	[[Category: Porcine aminopeptidase n]]

OCA at 08:33, 5 April 2017

2017-04-05T08:33:56Z

←Older revision		Revision as of 08:33, 5 April 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5lg6 is ON HOLD ~~until sometime in the future~~	+	The entry 5lg6 is ON HOLD

-	Authors: Santiago, ~~Cesar~~, Reguera, ~~Juan~~, Mudgal, ~~Gaurav~~, Casasnovas, ~~Jose~~ M.	+	Authors: Santiago, C., Reguera, J., Mudgal, G., Casasnovas, J.M.

-	Description: Structure of deglycosylated porcine aminopeptidase N	+	Description: Structure of the deglycosylated porcine aminopeptidase N ectodomain
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Santiago, Cesar,~~ Reguera, ~~Juan~~, Mudgal, ~~Gaurav~~, ~~Casasnovas, Jose M~~]]	+	[[Category: Reguera, J]]
		+	[[Category: Casasnovas, J.M]]
		+	[[Category: Mudgal, G]]
		+	[[Category: Santiago, C]]

OCA at 13:54, 27 July 2016

2016-07-27T13:54:54Z

←Older revision		Revision as of 13:54, 27 July 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5lg6 is ON HOLD	+	The entry 5lg6 is ON HOLD until sometime in the future

	Authors: Santiago, Cesar, Reguera, Juan, Mudgal, Gaurav, Casasnovas, Jose M.		Authors: Santiago, Cesar, Reguera, Juan, Mudgal, Gaurav, Casasnovas, Jose M.

OCA: Protected "5lg6" [edit=sysop:move=sysop]

2016-07-14T10:05:55Z

Protected "5lg6" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:05, 14 July 2016

OCA: New page: '''Unreleased structure''' The entry 5lg6 is ON HOLD Authors: Santiago, Cesar, Reguera, Juan, Mudgal, Gaurav, Casasnovas, Jose M. Description: Structure of deglycosylated porcine amino...

2016-07-14T10:05:53Z

New page: '''Unreleased structure''' The entry 5lg6 is ON HOLD Authors: Santiago, Cesar, Reguera, Juan, Mudgal, Gaurav, Casasnovas, Jose M. Description: Structure of deglycosylated porcine amino...

New page

'''Unreleased structure'''

The entry 5lg6 is ON HOLD

Authors: Santiago, Cesar, Reguera, Juan, Mudgal, Gaurav, Casasnovas, Jose M.

Description: Structure of deglycosylated porcine aminopeptidase N
[[Category: Unreleased Structures]]
[[Category: Santiago, Cesar, Reguera, Juan, Mudgal, Gaurav, Casasnovas, Jose M]]