5j5e: Difference between revisions

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'''Unreleased structure'''


The entry 5j5e is ON HOLD
==crystal structure of antigen-ERAP1 domain complex==
<StructureSection load='5j5e' size='340' side='right' caption='[[5j5e]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5j5e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J5E FirstGlance]. <br>
</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=5j5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j5e OCA], [http://pdbe.org/5j5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j5e RCSB], [http://www.ebi.ac.uk/pdbsum/5j5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j5e ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Endoplasmic reticulum aminopeptidase 1 (ERAP1) is an essential component of the immune system, because it trims peptide precursors and generates the N--restricted epitopes. To examine ERAP1's unique properties of length- and sequence-dependent processing of antigen precursors, we report a 2.3 A resolution complex structure of the ERAP1 regulatory domain. Our study reveals a binding conformation of ERAP1 to the carboxyl terminus of a peptide, and thus provides direct evidence for the molecular ruler mechanism.


Authors:  
Structural insights into the molecular ruler mechanism of the endoplasmic reticulum aminopeptidase ERAP1.,Gandhi A, Lakshminarasimhan D, Sun Y, Guo HC Sci Rep. 2011;1:186. Epub 2011 Dec 13. PMID:22355701<ref>PMID:22355701</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5j5e" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gandhi, A]]
[[Category: Guo, H C]]
[[Category: Sui, L]]
[[Category: Aminopeptidase]]
[[Category: Hydrolase]]
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