5k1v
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Endoplasmic Reticulum aminopeptidase 2 (ERAP2) in complex with a diaminobenzoic acid derivative ligand.== | |
| - | + | <StructureSection load='5k1v' size='340' side='right' caption='[[5k1v]], [[Resolution|resolution]] 2.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5k1v]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K1V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K1V FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6PX:METHYL+N-[4-AMINO-3-(L-ARGINYLAMINO)BENZENE-1-CARBONYL]-L-TYROSINATE'>6PX</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k1v OCA], [http://pdbe.org/5k1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k1v RCSB], [http://www.ebi.ac.uk/pdbsum/5k1v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k1v ProSAT]</span></td></tr> |
| - | [[ | + | </table> |
| - | [[ | + | == Function == |
| + | [[http://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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Giastas, P]] | [[Category: Giastas, P]] | ||
| + | [[Category: Mavridis, I M]] | ||
[[Category: Mpakali, A]] | [[Category: Mpakali, A]] | ||
| + | [[Category: Papakyriakou, A]] | ||
| + | [[Category: Saridakis, E]] | ||
[[Category: Stratikos, E]] | [[Category: Stratikos, E]] | ||
| - | [[Category: | + | [[Category: Diaminobenzoic acid derivative]] |
| + | [[Category: Endoplasmic reticulum aminopeptidase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Zinc-binding metallopeptidase]] | ||
Revision as of 13:46, 29 March 2017
Crystal structure of Endoplasmic Reticulum aminopeptidase 2 (ERAP2) in complex with a diaminobenzoic acid derivative ligand.
| |||||||||||
