5lhd - Revision history

OCA at 18:25, 18 October 2023

OCA — Wed, 18 Oct 2023 18:25:50 GMT

←Older revision		Revision as of 18:25, 18 October 2023
Line 3:		Line 3:
	<StructureSection load='5lhd' size='340' side='right'caption='[[5lhd]], [[Resolution\|resolution]] 2.60Å' scene=''>		<StructureSection load='5lhd' size='340' side='right'caption='[[5lhd]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lhd]] 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=5LHD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5LHD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lhd]] 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=5LHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LHD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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]] 2.6Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ANPEP, APN, CD13, PEPN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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'>[https://proteopedia.org/fgij/fg.htm?mol=5lhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhd OCA], [https://pdbe.org/5lhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lhd RCSB], [https://www.ebi.ac.uk/pdbsum/5lhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhd 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=5lhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhd OCA], [~~http~~://pdbe.org/5lhd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5lhd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5lhd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhd ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/AMPN_HUMAN AMPN_HUMAN]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. 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. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.<ref>PMID:1350662</ref> <ref>PMID:8105105</ref> <ref>PMID:8887485</ref> <ref>PMID:9056417</ref> <ref>PMID:9634079</ref> <ref>PMID:10605003</ref> <ref>PMID:10676659</ref> <ref>PMID:11384645</ref> <ref>PMID:12473585</ref>	+	[https://www.uniprot.org/uniprot/AMPN_HUMAN AMPN_HUMAN] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. 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. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.<ref>PMID:1350662</ref> <ref>PMID:8105105</ref> <ref>PMID:8887485</ref> <ref>PMID:9056417</ref> <ref>PMID:9634079</ref> <ref>PMID:10605003</ref> <ref>PMID:10676659</ref> <ref>PMID:11384645</ref> <ref>PMID:12473585</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Membrane alanyl aminopeptidase]]~~	+	[[Category: Casasnovas JM]]
-	[[Category: Casasnovas~~, J M~~]]	+	[[Category: Mudgal G]]
-	[[Category: Mudgal, G]]	+	[[Category: Recacha R]]
-	[[Category: Recacha, R]]	+	[[Category: Santiago C]]
-	[[Category: Santiago, C]]	+
-	~~[[Category: Cd13]]~~	+
-	~~[[Category: Human aminopeptidase n]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Metalloprotease~~]]	+

OCA at 06:29, 16 October 2019

OCA — Wed, 16 Oct 2019 06:29:10 GMT

←Older revision		Revision as of 06:29, 16 October 2019
Line 1:		Line 1:

	==Structure of glycosylated human aminopeptidase N==		==Structure of glycosylated human aminopeptidase N==
-	<StructureSection load='5lhd' size='340' side='right' caption='[[5lhd]], [[Resolution\|resolution]] 2.60Å' scene=''>	+	<StructureSection load='5lhd' size='340' side='right'caption='[[5lhd]], [[Resolution\|resolution]] 2.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lhd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LHD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lhd]] 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=5LHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LHD FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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, APN, CD13, PEPN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5lhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhd OCA], [http://pdbe.org/5lhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lhd RCSB], [http://www.ebi.ac.uk/pdbsum/5lhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhd 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=5lhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhd OCA], [http://pdbe.org/5lhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lhd RCSB], [http://www.ebi.ac.uk/pdbsum/5lhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhd ProSAT]</span></td></tr>
Line 19:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 5lhd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5lhd" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Aminopeptidase 3D structures\|Aminopeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Membrane alanyl aminopeptidase]]		[[Category: Membrane alanyl aminopeptidase]]
	[[Category: Casasnovas, J M]]		[[Category: Casasnovas, J M]]

OCA at 06:17, 19 April 2017

OCA — Wed, 19 Apr 2017 06:17:41 GMT

←Older revision		Revision as of 06:17, 19 April 2017
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/AMPN_HUMAN AMPN_HUMAN]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. 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. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.<ref>PMID:1350662</ref> <ref>PMID:8105105</ref> <ref>PMID:8887485</ref> <ref>PMID:9056417</ref> <ref>PMID:9634079</ref> <ref>PMID:10605003</ref> <ref>PMID:10676659</ref> <ref>PMID:11384645</ref> <ref>PMID:12473585</ref>		[[http://www.uniprot.org/uniprot/AMPN_HUMAN AMPN_HUMAN]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. 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. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.<ref>PMID:1350662</ref> <ref>PMID:8105105</ref> <ref>PMID:8887485</ref> <ref>PMID:9056417</ref> <ref>PMID:9634079</ref> <ref>PMID:10605003</ref> <ref>PMID:10676659</ref> <ref>PMID:11384645</ref> <ref>PMID:12473585</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 5lhd" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:27, 5 April 2017

OCA — Wed, 05 Apr 2017 13:27:57 GMT

←Older revision		Revision as of 13:27, 5 April 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5lhd is ~~ON HOLD~~	+	==Structure of glycosylated human aminopeptidase N==
-		+	<StructureSection load='5lhd' size='340' side='right' caption='[[5lhd]], [[Resolution\|resolution]] 2.60Å' scene=''>
-	~~Authors~~: ~~Recacha~~, R., ~~Mudgal~~, G., ~~Santiago~~, C., ~~Casasnovas, J~~.M.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5lhd]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LHD FirstGlance]. <br>
-	~~Description~~: ~~Structure~~ of ~~glycosylated~~ human aminopeptidase N	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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='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=5lhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhd OCA], [http://pdbe.org/5lhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lhd RCSB], [http://www.ebi.ac.uk/pdbsum/5lhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhd ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AMPN_HUMAN AMPN_HUMAN]] Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. 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. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection.<ref>PMID:1350662</ref> <ref>PMID:8105105</ref> <ref>PMID:8887485</ref> <ref>PMID:9056417</ref> <ref>PMID:9634079</ref> <ref>PMID:10605003</ref> <ref>PMID:10676659</ref> <ref>PMID:11384645</ref> <ref>PMID:12473585</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Membrane alanyl aminopeptidase]]
		+	[[Category: Casasnovas, J M]]
		+	[[Category: Mudgal, G]]
	[[Category: Recacha, R]]		[[Category: Recacha, R]]
-	[[Category: Casasnovas, J.M]]
-	[[Category: Mudgal, G]]
	[[Category: Santiago, C]]		[[Category: Santiago, C]]
		+	[[Category: Cd13]]
		+	[[Category: Human aminopeptidase n]]
		+	[[Category: Hydrolase]]
		+	[[Category: Metalloprotease]]

OCA at 10:40, 9 March 2017

OCA — Thu, 09 Mar 2017 10:40:25 GMT

←Older revision		Revision as of 10:40, 9 March 2017
Line 7:		Line 7:
	Description: Structure of glycosylated human aminopeptidase N		Description: Structure of glycosylated human aminopeptidase N
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Casasnovas, J.M]]
-	[[Category: Santiago, C]]
	[[Category: Recacha, R]]		[[Category: Recacha, R]]
		+	[[Category: Casasnovas, J.M]]
	[[Category: Mudgal, G]]		[[Category: Mudgal, G]]
		+	[[Category: Santiago, C]]

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

OCA — Tue, 26 Jul 2016 13:31:29 GMT

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

←Older revision

Revision as of 13:31, 26 July 2016

OCA: New page: '''Unreleased structure''' The entry 5lhd is ON HOLD Authors: Recacha, R., Mudgal, G., Santiago, C., Casasnovas, J.M. Description: Structure of glycosylated human aminopeptidase N [[Ca...

OCA — Tue, 26 Jul 2016 13:31:27 GMT

New page: '''Unreleased structure''' The entry 5lhd is ON HOLD Authors: Recacha, R., Mudgal, G., Santiago, C., Casasnovas, J.M. Description: Structure of glycosylated human aminopeptidase N [[Ca...

New page

'''Unreleased structure'''

The entry 5lhd is ON HOLD

Authors: Recacha, R., Mudgal, G., Santiago, C., Casasnovas, J.M.

Description: Structure of glycosylated human aminopeptidase N
[[Category: Unreleased Structures]]
[[Category: Casasnovas, J.M]]
[[Category: Santiago, C]]
[[Category: Recacha, R]]
[[Category: Mudgal, G]]