3qnf

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<StructureSection load='3qnf' size='340' side='right'caption='[[3qnf]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3qnf' size='340' side='right'caption='[[3qnf]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qnf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xdt|2xdt]]</div></td></tr>
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<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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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>
<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>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Endoplasmatic reticulum aminopeptidase 1 (ERAP1) is a multifunctional enzyme involved in trimming of peptides to an optimal length for presentation by major histocompatibility complex (MHC) class I molecules. Polymorphisms in ERAP1 have been associated with chronic inflammatory diseases, including ankylosing spondylitis (AS) and psoriasis, and subsequent in vitro enzyme studies suggest distinct catalytic properties of ERAP1 variants. To understand structure-activity relationships of this enzyme we determined crystal structures in open and closed states of human ERAP1, which provide the first snapshots along a catalytic path. ERAP1 is a zinc-metallopeptidase with typical H-E-X-X-H-(X)(18)-E zinc binding and G-A-M-E-N motifs characteristic for members of the gluzincin protease family. The structures reveal extensive domain movements, including an active site closure as well as three different open conformations, thus providing insights into the catalytic cycle. A K(528)R mutant strongly associated with AS in GWAS studies shows significantly altered peptide processing characteristics, which are possibly related to impaired interdomain interactions.
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Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.,Kochan G, Krojer T, Harvey D, Fischer R, Chen L, Vollmar M, von Delft F, Kavanagh KL, Brown MA, Bowness P, Wordsworth P, Kessler BM, Oppermann U Proc Natl Acad Sci U S A. 2011 May 10;108(19):7745-50. Epub 2011 Apr 20. PMID:21508329<ref>PMID:21508329</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qnf" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Allerston, C]]
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[[Category: Allerston C]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Berridge, G]]
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[[Category: Berridge G]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Chaikuad, A]]
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[[Category: Chaikuad A]]
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[[Category: Delft, F von]]
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[[Category: Edwards A]]
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[[Category: Edwards, A]]
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[[Category: Harvey D]]
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[[Category: Harvey, D]]
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[[Category: Kavanagh K]]
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[[Category: Kavanagh, K]]
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[[Category: Kochan G]]
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[[Category: Kochan, G]]
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[[Category: Krojer T]]
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[[Category: Krojer, T]]
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[[Category: Muniz JRC]]
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[[Category: Muniz, J R.C]]
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[[Category: Oppermann U]]
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[[Category: Oppermann, U]]
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[[Category: Raynor J]]
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[[Category: Raynor, J]]
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[[Category: Ugochukwu E]]
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[[Category: Structural genomic]]
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[[Category: Vollmar M]]
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[[Category: Ugochukwu, E]]
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[[Category: Wordsworth BP]]
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[[Category: Vollmar, M]]
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[[Category: Von Delft F]]
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[[Category: Wordsworth, B P]]
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[[Category: Adaptive immunity]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Metal-binding]]
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[[Category: Metalloprotease]]
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[[Category: Protease]]
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[[Category: Sgc]]
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Revision as of 11:52, 14 March 2024

Crystal structure of the open state of human endoplasmic reticulum aminopeptidase 1 ERAP1

PDB ID 3qnf

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