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| | ==Insulin regulated aminopeptidase== | | ==Insulin regulated aminopeptidase== |
| - | <StructureSection load='5c97' size='340' side='right' caption='[[5c97]], [[Resolution|resolution]] 3.37Å' scene=''> | + | <StructureSection load='5c97' size='340' side='right'caption='[[5c97]], [[Resolution|resolution]] 3.37Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c97]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C97 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c97]] is a 2 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=5C97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C97 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.37Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4z7i|4z7i]], [[4p8q|4p8q]], [[4pj6|4pj6]]</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></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cystinyl_aminopeptidase Cystinyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.3 3.4.11.3] </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=5c97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c97 OCA], [https://pdbe.org/5c97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c97 RCSB], [https://www.ebi.ac.uk/pdbsum/5c97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c97 ProSAT]</span></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=5c97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c97 OCA], [http://pdbe.org/5c97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c97 RCSB], [http://www.ebi.ac.uk/pdbsum/5c97 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LCAP_HUMAN LCAP_HUMAN]] Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain.<ref>PMID:11389728</ref> <ref>PMID:11707427</ref> <ref>PMID:1731608</ref> | + | [https://www.uniprot.org/uniprot/LCAP_HUMAN LCAP_HUMAN] Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain.<ref>PMID:11389728</ref> <ref>PMID:11707427</ref> <ref>PMID:1731608</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5c97" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5c97" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cystinyl aminopeptidase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Harlos, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Mpakali, A]] | + | [[Category: Harlos K]] |
| - | [[Category: Saridakis, E]] | + | [[Category: Mpakali A]] |
| - | [[Category: Stratikos, E]] | + | [[Category: Saridakis E]] |
| - | [[Category: Zhao, Y]] | + | [[Category: Stratikos E]] |
| - | [[Category: Aminopeptidase]]
| + | [[Category: Zhao Y]] |
| - | [[Category: Antigen presentation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Irap]]
| + | |
| Structural highlights
Function
LCAP_HUMAN Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain.[1] [2] [3]
Publication Abstract from PubMed
Aminopeptidases that generate antigenic peptides influence immunodominance and adaptive cytotoxic immune responses. The mechanisms that allow these enzymes to efficiently process a vast number of different long peptide substrates are poorly understood. In this work, we report the structure of insulin-regulated aminopeptidase, an enzyme that prepares antigenic epitopes for cross-presentation in dendritic cells, in complex with an antigenic peptide precursor analog. Insulin-regulated aminopeptidase is found in a semiclosed conformation with an extended internal cavity with limited access to the solvent. The N-terminal moiety of the peptide is located at the active site, positioned optimally for catalysis, whereas the C-terminal moiety of the peptide is stabilized along the extended internal cavity lodged between domains II and IV. Hydrophobic interactions and shape complementarity enhance peptide affinity beyond the catalytic site and support a limited selectivity model for antigenic peptide selection that may underlie the generation of complex immunopeptidomes.
Crystal Structure of Insulin-Regulated Aminopeptidase with Bound Substrate Analogue Provides Insight on Antigenic Epitope Precursor Recognition and Processing.,Mpakali A, Saridakis E, Harlos K, Zhao Y, Papakyriakou A, Kokkala P, Georgiadis D, Stratikos E J Immunol. 2015 Aug 10. pii: 1501103. PMID:26259583[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Matsumoto H, Nagasaka T, Hattori A, Rogi T, Tsuruoka N, Mizutani S, Tsujimoto M. Expression of placental leucine aminopeptidase/oxytocinase in neuronal cells and its action on neuronal peptides. Eur J Biochem. 2001 Jun;268(11):3259-66. PMID:11389728
- ↑ Albiston AL, McDowall SG, Matsacos D, Sim P, Clune E, Mustafa T, Lee J, Mendelsohn FA, Simpson RJ, Connolly LM, Chai SY. Evidence that the angiotensin IV (AT(4)) receptor is the enzyme insulin-regulated aminopeptidase. J Biol Chem. 2001 Dec 28;276(52):48623-6. Epub 2001 Nov 13. PMID:11707427 doi:http://dx.doi.org/10.1074/jbc.C100512200
- ↑ Tsujimoto M, Mizutani S, Adachi H, Kimura M, Nakazato H, Tomoda Y. Identification of human placental leucine aminopeptidase as oxytocinase. Arch Biochem Biophys. 1992 Feb 1;292(2):388-92. PMID:1731608
- ↑ Mpakali A, Saridakis E, Harlos K, Zhao Y, Papakyriakou A, Kokkala P, Georgiadis D, Stratikos E. Crystal Structure of Insulin-Regulated Aminopeptidase with Bound Substrate Analogue Provides Insight on Antigenic Epitope Precursor Recognition and Processing. J Immunol. 2015 Aug 10. pii: 1501103. PMID:26259583 doi:http://dx.doi.org/10.4049/jimmunol.1501103
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