4jbs
From Proteopedia
(Difference between revisions)
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- | + | {{STRUCTURE_4jbs| PDB=4jbs | SCENE= }} | |
+ | ===Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2 in complex with PHOSPHINIC PSEUDOTRIPEPTIDE inhibitor.=== | ||
+ | {{ABSTRACT_PUBMED_24248368}} | ||
- | + | ==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> | ||
- | + | ==About this Structure== | |
+ | [[4jbs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JBS OCA]. | ||
- | + | ==Reference== | |
+ | <ref group="xtra">PMID:024248368</ref><references group="xtra"/><references/> | ||
+ | [[Category: Birtley, J.]] | ||
+ | [[Category: Mavridis, I M.]] | ||
+ | [[Category: Saridakis, E.]] | ||
+ | [[Category: Stratikos, E.]] | ||
+ | [[Category: Aminopeptidase]] | ||
+ | [[Category: Endoplasmic reticulum]] | ||
+ | [[Category: Hydrolase]] | ||
+ | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
+ | [[Category: Thermolysin-like catalytic domain]] | ||
+ | [[Category: Zinc binding]] |
Revision as of 13:35, 11 December 2013
Contents |
Crystal structure of the human Endoplasmic Reticulum Aminopeptidase 2 in complex with PHOSPHINIC PSEUDOTRIPEPTIDE inhibitor.
Template:ABSTRACT PUBMED 24248368
Function
[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.[1] [2] [3]
About this Structure
4jbs is a 2 chain structure. Full crystallographic information is available from OCA.
Reference
- Zervoudi E, Saridakis E, Birtley JR, Seregin SS, Reeves E, Kokkala P, Aldhamen YA, Amalfitano A, Mavridis IM, James E, Georgiadis D, Stratikos E. Rationally designed inhibitor targeting antigen-trimming aminopeptidases enhances antigen presentation and cytotoxic T-cell responses. Proc Natl Acad Sci U S A. 2013 Dec 3;110(49):19890-5. doi:, 10.1073/pnas.1309781110. Epub 2013 Nov 18. PMID:24248368 doi:http://dx.doi.org/10.1073/pnas.1309781110
- ↑ Tanioka T, Hattori A, Masuda S, Nomura Y, Nakayama H, Mizutani S, Tsujimoto M. Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases. J Biol Chem. 2003 Aug 22;278(34):32275-83. Epub 2003 Jun 10. PMID:12799365 doi:http://dx.doi.org/10.1074/jbc.M305076200
- ↑ Saveanu L, Carroll O, Lindo V, Del Val M, Lopez D, Lepelletier Y, Greer F, Schomburg L, Fruci D, Niedermann G, van Endert PM. Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum. Nat Immunol. 2005 Jul;6(7):689-97. Epub 2005 May 22. PMID:15908954 doi:http://dx.doi.org/10.1038/ni1208
- ↑ Chang SC, Momburg F, Bhutani N, Goldberg AL. The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism. Proc Natl Acad Sci U S A. 2005 Nov 22;102(47):17107-12. Epub 2005 Nov 14. PMID:16286653 doi:http://dx.doi.org/0500721102