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5c97

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Revision as of 06:45, 30 September 2015

Insulin regulated aminopeptidase

Structural highlights

5c97 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4z7i, 4p8q, 4pj6
Activity:	Cystinyl aminopeptidase, with EC number 3.4.11.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5c97"

@@ Line 6: / Line 6: @@
 <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='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'>[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://www.rcsb.org/pdb/explore.do?structureId=5c97 RCSB], [http://www.ebi.ac.uk/pdbsum/5c97 PDBsum]</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>
 == Function ==
@@ Line 18: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 5c97" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

5c97

From Proteopedia

Revision as of 06:45, 30 September 2015

Insulin regulated aminopeptidase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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