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3se6
From Proteopedia
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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=3se6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3se6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3se6 RCSB], [http://www.ebi.ac.uk/pdbsum/3se6 PDBsum]</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=3se6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3se6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3se6 RCSB], [http://www.ebi.ac.uk/pdbsum/3se6 PDBsum]</span></td></tr> | ||
</table> | </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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 03:06, 25 December 2014
Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2
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