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.


5al2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:12, 10 January 2024) (edit) (undo)
 
(4 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of TNKS2 in complex with 2-(4-(propan-2-yl)phenyl)- 1H,2H,3H,4H-pyrido(2,3-d)pyrimidin-4-one==
==Crystal structure of TNKS2 in complex with 2-(4-(propan-2-yl)phenyl)- 1H,2H,3H,4H-pyrido(2,3-d)pyrimidin-4-one==
-
<StructureSection load='5al2' size='340' side='right' caption='[[5al2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+
<StructureSection load='5al2' size='340' side='right'caption='[[5al2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5al2]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AL2 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5al2]] 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=5AL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AL2 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=O53:(2S)-2-(4-PROPAN-2-YLPHENYL)-2,3-DIHYDRO-1H-PYRIDO[2,3-D]PYRIMIDIN-4-ONE'>O53</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.9&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aku|5aku]], [[5akw|5akw]], [[5al1|5al1]], [[5al3|5al3]], [[5al4|5al4]], [[5al5|5al5]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=O53:(2S)-2-(4-PROPAN-2-YLPHENYL)-2,3-DIHYDRO-1H-PYRIDO[2,3-D]PYRIMIDIN-4-ONE'>O53</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5al2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5al2 OCA], [https://pdbe.org/5al2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5al2 RCSB], [https://www.ebi.ac.uk/pdbsum/5al2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5al2 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=5al2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5al2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5al2 RCSB], [http://www.ebi.ac.uk/pdbsum/5al2 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 5al2" 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: Lehtio, L]]
+
[[Category: Homo sapiens]]
-
[[Category: Nkizinkiko, Y]]
+
[[Category: Large Structures]]
-
[[Category: Adp- ribosylation]]
+
[[Category: Lehtio L]]
-
[[Category: Diphtheria toxin like fold]]
+
[[Category: Nkizinkiko Y]]
-
[[Category: Protein-ligand complex]]
+
-
[[Category: Transferase]]
+
-
[[Category: Transferase-transferase inhibitor complex]]
+

Current revision

Crystal structure of TNKS2 in complex with 2-(4-(propan-2-yl)phenyl)- 1H,2H,3H,4H-pyrido(2,3-d)pyrimidin-4-one

PDB ID 5al2

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/5al2"
Personal tools