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| | ==Human ARTD15/PARP16 IN COMPLEX WITH 3-AMINOBENZAMIDE== | | ==Human ARTD15/PARP16 IN COMPLEX WITH 3-AMINOBENZAMIDE== |
| - | <StructureSection load='4f0d' size='340' side='right' caption='[[4f0d]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4f0d' size='340' side='right'caption='[[4f0d]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4f0d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F0D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F0D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4f0d]] 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=4F0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F0D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3AB:3-AMINOBENZAMIDE'>3AB</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3AB:3-AMINOBENZAMIDE'>3AB</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C15orf30, PARP16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4f0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f0d OCA], [https://pdbe.org/4f0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f0d RCSB], [https://www.ebi.ac.uk/pdbsum/4f0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f0d ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </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=4f0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f0d OCA], [http://pdbe.org/4f0d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f0d RCSB], [http://www.ebi.ac.uk/pdbsum/4f0d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f0d ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PAR16_HUMAN PAR16_HUMAN]] Mono-ADP-ribosyltransferase targeting the karyopherin KPNB1. Plays a role in unfolded protein response (UPR), by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors.<ref>PMID:23103912</ref> <ref>PMID:22701565</ref> | + | [https://www.uniprot.org/uniprot/PAR16_HUMAN PAR16_HUMAN] Mono-ADP-ribosyltransferase targeting the karyopherin KPNB1. Plays a role in unfolded protein response (UPR), by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors.<ref>PMID:23103912</ref> <ref>PMID:22701565</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Poly (ADP-ribose) polymerase|Poly (ADP-ribose) polymerase]] | + | *[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Kallas, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Karlberg, T]] | + | [[Category: Kallas A]] |
| - | [[Category: Structural genomic]] | + | [[Category: Karlberg T]] |
| - | [[Category: Schuler, H]] | + | [[Category: Schuler H]] |
| - | [[Category: Thorsell, A G]] | + | [[Category: Thorsell AG]] |
| - | [[Category: Adp-ribose]]
| + | |
| - | [[Category: Adp-ribosylation]]
| + | |
| - | [[Category: Artd transferase domain]]
| + | |
| - | [[Category: Artd15]]
| + | |
| - | [[Category: Parp16]]
| + | |
| - | [[Category: Sgc]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Transferase-transferase inhibitor complex]]
| + | |
| Structural highlights
Function
PAR16_HUMAN Mono-ADP-ribosyltransferase targeting the karyopherin KPNB1. Plays a role in unfolded protein response (UPR), by ADP-ribosylating and activating EIF2AK3 and ERN1, two important UPR effectors.[1] [2]
Publication Abstract from PubMed
ADP-ribosylation is involved in the regulation of DNA repair, transcription, and other processes. The 18 human ADP-ribose transferases with diphtheria toxin homology include ARTD1/PARP1, a cancer drug target. Knowledge of other family members may guide therapeutics development and help evaluate potential drug side effects. Here, we present the crystal structure of human ARTD15/PARP16, a previously uncharacterized enzyme. ARTD15 features an alpha-helical domain that packs against its transferase domain without making direct contact with the NAD(+)-binding crevice or the donor loop. Thus, this novel domain does not resemble the regulatory domain of ARTD1. ARTD15 displays auto-mono(ADP-ribosylation) activity and is affected by canonical poly(ADP-ribose) polymerase inhibitors. These results add to a framework that will facilitate research on a medically important family of enzymes.
Crystal Structure of Human ADP-ribose Transferase ARTD15/PARP16 Reveals a Novel Putative Regulatory Domain.,Karlberg T, Thorsell AG, Kallas A, Schuler H J Biol Chem. 2012 Jul 13;287(29):24077-81. Epub 2012 Jun 1. PMID:22661712[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jwa M, Chang P. PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1alpha-mediated unfolded protein response. Nat Cell Biol. 2012 Nov;14(11):1223-30. doi: 10.1038/ncb2593. Epub 2012 Oct 28. PMID:23103912 doi:http://dx.doi.org/10.1038/ncb2593
- ↑ Di Paola S, Micaroni M, Di Tullio G, Buccione R, Di Girolamo M. PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ss1. PLoS One. 2012;7(6):e37352. doi: 10.1371/journal.pone.0037352. Epub 2012 Jun 11. PMID:22701565 doi:http://dx.doi.org/10.1371/journal.pone.0037352
- ↑ Karlberg T, Thorsell AG, Kallas A, Schuler H. Crystal Structure of Human ADP-ribose Transferase ARTD15/PARP16 Reveals a Novel Putative Regulatory Domain. J Biol Chem. 2012 Jul 13;287(29):24077-81. Epub 2012 Jun 1. PMID:22661712 doi:10.1074/jbc.M112.379289
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