5lhd

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'''Unreleased structure'''
 
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The entry 5lhd is ON HOLD
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==Structure of glycosylated human aminopeptidase N==
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<StructureSection load='5lhd' size='340' side='right' caption='[[5lhd]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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Authors: Recacha, R., Mudgal, G., Santiago, C., Casasnovas, J.M.
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== Structural highlights ==
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<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>
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Description: Structure of glycosylated human aminopeptidase N
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</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>
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[[Category: Unreleased Structures]]
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<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>
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<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>
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</table>
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== Function ==
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[[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Membrane alanyl aminopeptidase]]
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[[Category: Casasnovas, J M]]
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[[Category: Mudgal, G]]
[[Category: Recacha, R]]
[[Category: Recacha, R]]
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[[Category: Casasnovas, J.M]]
 
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[[Category: Mudgal, G]]
 
[[Category: Santiago, C]]
[[Category: Santiago, C]]
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[[Category: Cd13]]
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[[Category: Human aminopeptidase n]]
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[[Category: Hydrolase]]
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[[Category: Metalloprotease]]

Revision as of 13:27, 5 April 2017

Structure of glycosylated human aminopeptidase N

5lhd, resolution 2.60Å

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