5k1v: Difference between revisions

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'''Unreleased structure'''


The entry 5k1v is ON HOLD  until Paper Publication
==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]] 2.90&Aring;' scene=''>
Authors: Saridakis, E., Papakyriakou, A., Giastas, P., Mpakali, A., Mavridis, I.M., Stratikos, E.
== 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>
Description: Crystal structure of Endoplasmic Reticulum aminopeptidase 2 (ERAP2) in complex with a diaminobenzoic acid derivative ligand.
</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>
[[Category: Unreleased Structures]]
<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>
[[Category: Saridakis, E]]
</table>
[[Category: Papakyriakou, A]]
== 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: Mavridis, I.M]]
[[Category: Diaminobenzoic acid derivative]]
[[Category: Endoplasmic reticulum aminopeptidase]]
[[Category: Hydrolase]]
[[Category: Zinc-binding metallopeptidase]]