This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4tkg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:46, 28 December 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal Structure of human Tankyrase 2 in complex with AZD2281.==
==Crystal Structure of human Tankyrase 2 in complex with AZD2281.==
-
<StructureSection load='4tkg' size='340' side='right' caption='[[4tkg]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+
<StructureSection load='4tkg' size='340' side='right'caption='[[4tkg]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4tkg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TKG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TKG FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4tkg]] is a 4 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=4TKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TKG FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=09L:4-(3-{[4-(CYCLOPROPYLCARBONYL)PIPERAZIN-1-YL]CARBONYL}-4-FLUOROBENZYL)PHTHALAZIN-1(2H)-ONE'>09L</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pml|4pml]], [[4pnl|4pnl]], [[4pnm|4pnm]], [[4pnn|4pnn]], [[4pnq|4pnq]], [[4pnt|4pnt]], [[4pnr|4pnr]], [[4pns|4pns]], [[4tju|4tju]], [[4tjw|4tjw]], [[4tjy|4tjy]], [[4tk0|4tk0]], [[4tk5|4tk5]], [[4tkf|4tkf]], [[4tki|4tki]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=09L:4-(3-{[4-(CYCLOPROPYLCARBONYL)PIPERAZIN-1-YL]CARBONYL}-4-FLUOROBENZYL)PHTHALAZIN-1(2H)-ONE'>09L</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4tkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tkg OCA], [https://pdbe.org/4tkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tkg RCSB], [https://www.ebi.ac.uk/pdbsum/4tkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tkg ProSAT]</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=4tkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tkg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tkg RCSB], [http://www.ebi.ac.uk/pdbsum/4tkg PDBsum]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/TNKS2_HUMAN TNKS2_HUMAN]] Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles.<ref>PMID:11802774</ref> <ref>PMID:11739745</ref> <ref>PMID:19759537</ref> <ref>PMID:21478859</ref>
+
[https://www.uniprot.org/uniprot/TNKS2_HUMAN TNKS2_HUMAN] Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles.<ref>PMID:11802774</ref> <ref>PMID:11739745</ref> <ref>PMID:19759537</ref> <ref>PMID:21478859</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 18: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 4tkg" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Battaile, K P]]
+
[[Category: Homo sapiens]]
-
[[Category: Beletskaya, I]]
+
[[Category: Large Structures]]
-
[[Category: Chirgadze, N Y]]
+
[[Category: Battaile KP]]
-
[[Category: Gebremeskel, S]]
+
[[Category: Beletskaya I]]
-
[[Category: Gordon, R]]
+
[[Category: Chirgadze NY]]
-
[[Category: Lam, R]]
+
[[Category: Gebremeskel S]]
-
[[Category: Pai, E F]]
+
[[Category: Gordon R]]
-
[[Category: Qiu, W]]
+
[[Category: Lam R]]
-
[[Category: Romanov, V]]
+
[[Category: Pai EF]]
-
[[Category: Thompson, C]]
+
[[Category: Qiu W]]
-
[[Category: Vodsedalek, J]]
+
[[Category: Romanov V]]
-
[[Category: Transferase]]
+
[[Category: Thompson C]]
 +
[[Category: Vodsedalek J]]

Current revision

Crystal Structure of human Tankyrase 2 in complex with AZD2281.

PDB ID 4tkg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4tkg"
Personal tools