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6mgq

From Proteopedia

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m (Protected "6mgq" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6mgq is ON HOLD until Paper Publication
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==ER aminopeptidase 1 bound to 10mer phosphinic inhibitor DG014==
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<StructureSection load='6mgq' size='340' side='right'caption='[[6mgq]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
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Authors: Stern, L.J., Maben, Z.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6mgq]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MGQ FirstGlance]. <br>
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Description: ER aminopeptidase 1 bound to 10mer phosphinic inhibitor DG014
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</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>
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[[Category: Unreleased Structures]]
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=2X0:[(1R)-1-AMINO-3-PHENYLPROPYL]PHOSPHONIC+ACID'>2X0</scene>, <scene name='pdbligand=7GA:2,4-DIMETHYLPENTANAL'>7GA</scene></td></tr>
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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=6mgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mgq OCA], [http://pdbe.org/6mgq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mgq RCSB], [http://www.ebi.ac.uk/pdbsum/6mgq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mgq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[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>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Maben, Z]]
[[Category: Maben, Z]]
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[[Category: Stern, L.J]]
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[[Category: Stern, L J]]
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[[Category: Aminopeptidase]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-inhibitor complex]]
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[[Category: Immune system]]
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[[Category: Inhibitor]]

Revision as of 07:42, 18 December 2019

ER aminopeptidase 1 bound to 10mer phosphinic inhibitor DG014

PDB ID 6mgq

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