View source for 3qnf


==Crystal structure of the open state of human endoplasmic reticulum aminopeptidase 1 ERAP1==
<StructureSection load='3qnf' size='340' side='right'caption='[[3qnf]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qnf]] is a 3 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=3QNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QNF 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=3qnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qnf OCA], [https://pdbe.org/3qnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qnf RCSB], [https://www.ebi.ac.uk/pdbsum/3qnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qnf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ERAP1_HUMAN ERAP1_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. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.<ref>PMID:15908954</ref> <ref>PMID:16286653</ref> <ref>PMID:21478864</ref> 

==See Also==
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Allerston C]]
[[Category: Arrowsmith CH]]
[[Category: Berridge G]]
[[Category: Bountra C]]
[[Category: Chaikuad A]]
[[Category: Edwards A]]
[[Category: Harvey D]]
[[Category: Kavanagh K]]
[[Category: Kochan G]]
[[Category: Krojer T]]
[[Category: Muniz JRC]]
[[Category: Oppermann U]]
[[Category: Raynor J]]
[[Category: Ugochukwu E]]
[[Category: Vollmar M]]
[[Category: Wordsworth BP]]
[[Category: Von Delft F]]