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4e36
From Proteopedia
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| - | [[Image:4e36.jpg|left|200px]] | ||
| - | + | ==Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2 variant N392K== | |
| + | <StructureSection load='4e36' size='340' side='right'caption='[[4e36]], [[Resolution|resolution]] 3.22Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4e36]] 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=4E36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E36 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.22Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4e36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e36 OCA], [https://pdbe.org/4e36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e36 RCSB], [https://www.ebi.ac.uk/pdbsum/4e36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e36 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ERAP2_HUMAN ERAP2_HUMAN] Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys.<ref>PMID:12799365</ref> <ref>PMID:15908954</ref> <ref>PMID:16286653</ref> | ||
| - | == | + | ==See Also== |
| - | + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | [[ | + | </StructureSection> |
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| - | == | + | |
| - | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Birtley | + | [[Category: Large Structures]] |
| - | [[Category: Mavridis | + | [[Category: Birtley JR]] |
| - | [[Category: Pegias | + | [[Category: Mavridis IM]] |
| - | [[Category: Saridakis | + | [[Category: Pegias P]] |
| - | [[Category: Stratikos | + | [[Category: Saridakis E]] |
| - | + | [[Category: Stratikos E]] | |
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Current revision
Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2 variant N392K
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