8sw0: Difference between revisions
New page: '''Unreleased structure''' The entry 8sw0 is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Puromycin sensitive aminopeptidase== | ||
<StructureSection load='8sw0' size='340' side='right'caption='[[8sw0]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8sw0]] is a 1 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=8SW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SW0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.301Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=8sw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sw0 OCA], [https://pdbe.org/8sw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sw0 RCSB], [https://www.ebi.ac.uk/pdbsum/8sw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sw0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PSA_HUMAN PSA_HUMAN] Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently than tau from Alzheimer disease brain.<ref>PMID:10978616</ref> <ref>PMID:11062501</ref> <ref>PMID:17154549</ref> <ref>PMID:17318184</ref> <ref>PMID:19917696</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Puromycin-sensitive aminopeptidase (E.C. 3.4.11.14, UniProt P55786), a zinc metallopeptidase belonging to the M1 family, degrades a number of bioactive peptides as well as peptides released from the proteasome, including polyglutamine. We report the crystal structure of PSA at 2.3 A. Overall, the enzyme adopts a V-shaped architecture with four domains characteristic of the M1 family aminopeptidases, but it is in a less compact conformation compared to most M1 enzymes of known structure. A microtubule binding sequence is present in a C-terminal HEAT repeat domain of the enzyme in a position where it might serve to mediate interaction with tubulin. In the catalytic metallopeptidase domain, an elongated active site groove lined with aromatic and hydrophobic residues and a large S1 subsite may play a role in broad substrate recognition. The structure with bound polyglutamine shows a possible interacting mode of this peptide, which is supported by mutation. | |||
Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.,Madabushi S, Chow KM, Song ES, Goswami A, Hersh LB, Rodgers DW PLoS One. 2023 Jul 13;18(7):e0287086. doi: 10.1371/journal.pone.0287086. , eCollection 2023. PMID:37440518<ref>PMID:37440518</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8sw0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Rodgers DW]] | |||
[[Category: Sampath S]] | |||
Latest revision as of 15:42, 26 July 2023
Puromycin sensitive aminopeptidasePuromycin sensitive aminopeptidase
Structural highlights
FunctionPSA_HUMAN Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently than tau from Alzheimer disease brain.[1] [2] [3] [4] [5] Publication Abstract from PubMedPuromycin-sensitive aminopeptidase (E.C. 3.4.11.14, UniProt P55786), a zinc metallopeptidase belonging to the M1 family, degrades a number of bioactive peptides as well as peptides released from the proteasome, including polyglutamine. We report the crystal structure of PSA at 2.3 A. Overall, the enzyme adopts a V-shaped architecture with four domains characteristic of the M1 family aminopeptidases, but it is in a less compact conformation compared to most M1 enzymes of known structure. A microtubule binding sequence is present in a C-terminal HEAT repeat domain of the enzyme in a position where it might serve to mediate interaction with tubulin. In the catalytic metallopeptidase domain, an elongated active site groove lined with aromatic and hydrophobic residues and a large S1 subsite may play a role in broad substrate recognition. The structure with bound polyglutamine shows a possible interacting mode of this peptide, which is supported by mutation. Structure of puromycin-sensitive aminopeptidase and polyglutamine binding.,Madabushi S, Chow KM, Song ES, Goswami A, Hersh LB, Rodgers DW PLoS One. 2023 Jul 13;18(7):e0287086. doi: 10.1371/journal.pone.0287086. , eCollection 2023. PMID:37440518[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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