4f0d

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==Human ARTD15/PARP16 IN COMPLEX WITH 3-AMINOBENZAMIDE==
==Human ARTD15/PARP16 IN COMPLEX WITH 3-AMINOBENZAMIDE==
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<StructureSection load='4f0d' size='340' side='right' caption='[[4f0d]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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<StructureSection load='4f0d' size='340' side='right'caption='[[4f0d]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4f0d]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F0D FirstGlance]. <br>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<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 Homo sapiens])</td></tr>
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<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>
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<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>
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<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>
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<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://www.rcsb.org/pdb/explore.do?structureId=4f0d RCSB], [http://www.ebi.ac.uk/pdbsum/4f0d PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:22661712</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
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*[[Poly (ADP-ribose) polymerase|Poly (ADP-ribose) polymerase]]
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*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Kallas, A]]
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[[Category: Large Structures]]
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[[Category: Karlberg, T]]
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[[Category: Kallas A]]
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[[Category: Structural genomic]]
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[[Category: Karlberg T]]
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[[Category: Schuler, H]]
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[[Category: Schuler H]]
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[[Category: Thorsell, A G]]
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[[Category: Thorsell AG]]
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[[Category: Adp-ribose]]
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[[Category: Adp-ribosylation]]
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[[Category: Artd transferase domain]]
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[[Category: Artd15]]
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[[Category: Parp16]]
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[[Category: Sgc]]
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[[Category: Transferase]]
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[[Category: Transferase-transferase inhibitor complex]]
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Current revision

Human ARTD15/PARP16 IN COMPLEX WITH 3-AMINOBENZAMIDE

PDB ID 4f0d

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