4abk: Difference between revisions
New page: '''Unreleased structure''' The entry 4abk is ON HOLD until sometime in the future Authors: KARLBERG, T., MOCHE, M., THORSELL, A.G., ARROWSMITH, C.H., BOUNTRA, C., EDWARDS, A.M., EKBLAD,... |
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==HUMAN PARP14 (ARTD8, BAL2) - MACRO DOMAIN 3 IN COMPLEX WITH ADENOSINE- 5-DIPHOSPHORIBOSE== | |||
<StructureSection load='4abk' size='340' side='right'caption='[[4abk]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4abk]] 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=4ABK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ABK 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]] 1.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AR6:[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL]+HYDROGEN+PHOSPHATE'>AR6</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=4abk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4abk OCA], [https://pdbe.org/4abk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4abk RCSB], [https://www.ebi.ac.uk/pdbsum/4abk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4abk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PAR14_HUMAN PAR14_HUMAN] Enhances STAT6-dependent transcription (By similarity). Has ADP-ribosyltransferase activity. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
ADP-ribosyltransferases (ARTs) catalyze the transfer of ADP-ribose from NAD onto substrates. Some ARTs generate in an iterative process ADP-ribose polymers that serve as adaptors for distinct protein domains. Other ARTs, exemplified by ARTD10, function as mono-ADP-ribosyltransferases, but it has been unclear whether this modification occurs in cells and how it is read. We observed that ARTD10 colocalized with ARTD8 and defined its macrodomains 2 and 3 as readers of mono-ADP-ribosylation both in vitro and in cells. The crystal structures of these two ARTD8 macrodomains and isothermal titration calorimetry confirmed their interaction with ADP-ribose. These macrodomains recognized mono-ADP-ribosylated ARTD10, but not poly-ADP-ribosylated ARTD1. This distinguished them from the macrodomain of macroH2A1.1, which interacted with poly- but not mono-ADP-ribosylated substrates. Moreover, Ran, an ARTD10 substrate, was also read by ARTD8 macrodomains. This identifies readers of mono-ADP-ribosylated proteins, defines their structures, and demonstrates the presence of this modification in cells. | |||
Recognition of Mono-ADP-Ribosylated ARTD10 Substrates by ARTD8 Macrodomains.,Forst AH, Karlberg T, Herzog N, Thorsell AG, Gross A, Feijs KL, Verheugd P, Kursula P, Nijmeijer B, Kremmer E, Kleine H, Ladurner AG, Schuler H, Luscher B Structure. 2013 Mar 5;21(3):462-75. doi: 10.1016/j.str.2012.12.019. PMID:23473667<ref>PMID:23473667</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4abk" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith CH]] | |||
[[Category: Bountra C]] | |||
[[Category: Edwards AM]] | |||
[[Category: Ekblad T]] | |||
[[Category: Karlberg T]] | |||
[[Category: Moche M]] | |||
[[Category: Schuler H]] | |||
[[Category: Thorsell AG]] | |||
[[Category: Weigelt J]] | |||
Latest revision as of 14:23, 20 December 2023
HUMAN PARP14 (ARTD8, BAL2) - MACRO DOMAIN 3 IN COMPLEX WITH ADENOSINE- 5-DIPHOSPHORIBOSEHUMAN PARP14 (ARTD8, BAL2) - MACRO DOMAIN 3 IN COMPLEX WITH ADENOSINE- 5-DIPHOSPHORIBOSE
Structural highlights
FunctionPAR14_HUMAN Enhances STAT6-dependent transcription (By similarity). Has ADP-ribosyltransferase activity. Publication Abstract from PubMedADP-ribosyltransferases (ARTs) catalyze the transfer of ADP-ribose from NAD onto substrates. Some ARTs generate in an iterative process ADP-ribose polymers that serve as adaptors for distinct protein domains. Other ARTs, exemplified by ARTD10, function as mono-ADP-ribosyltransferases, but it has been unclear whether this modification occurs in cells and how it is read. We observed that ARTD10 colocalized with ARTD8 and defined its macrodomains 2 and 3 as readers of mono-ADP-ribosylation both in vitro and in cells. The crystal structures of these two ARTD8 macrodomains and isothermal titration calorimetry confirmed their interaction with ADP-ribose. These macrodomains recognized mono-ADP-ribosylated ARTD10, but not poly-ADP-ribosylated ARTD1. This distinguished them from the macrodomain of macroH2A1.1, which interacted with poly- but not mono-ADP-ribosylated substrates. Moreover, Ran, an ARTD10 substrate, was also read by ARTD8 macrodomains. This identifies readers of mono-ADP-ribosylated proteins, defines their structures, and demonstrates the presence of this modification in cells. Recognition of Mono-ADP-Ribosylated ARTD10 Substrates by ARTD8 Macrodomains.,Forst AH, Karlberg T, Herzog N, Thorsell AG, Gross A, Feijs KL, Verheugd P, Kursula P, Nijmeijer B, Kremmer E, Kleine H, Ladurner AG, Schuler H, Luscher B Structure. 2013 Mar 5;21(3):462-75. doi: 10.1016/j.str.2012.12.019. PMID:23473667[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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