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4z68

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==Hybrid structural analysis of the Arp2/3 regulator Arpin identifies its acidic tail as a primary binding epitope==
==Hybrid structural analysis of the Arp2/3 regulator Arpin identifies its acidic tail as a primary binding epitope==
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<StructureSection load='4z68' size='340' side='right' caption='[[4z68]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
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<StructureSection load='4z68' size='340' side='right'caption='[[4z68]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4z68]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z68 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4z68]] 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=4Z68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z68 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=SO4:SULFATE+ION'>SO4</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]] 1.859&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4z68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z68 OCA], [http://pdbe.org/4z68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z68 RCSB], [http://www.ebi.ac.uk/pdbsum/4z68 PDBsum]</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=4z68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z68 OCA], [https://pdbe.org/4z68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z68 RCSB], [https://www.ebi.ac.uk/pdbsum/4z68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z68 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[https://www.uniprot.org/uniprot/ARPIN_HUMAN ARPIN_HUMAN] Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence.<ref>PMID:24132237</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4z68" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4z68" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Campanacci, V]]
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[[Category: Homo sapiens]]
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[[Category: Cherfils, J]]
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[[Category: Large Structures]]
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[[Category: Dang, I]]
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[[Category: Campanacci V]]
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[[Category: Fetics, S K]]
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[[Category: Cherfils J]]
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[[Category: Gautreau, A]]
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[[Category: Dang I]]
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[[Category: Actin polymerization]]
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[[Category: Fetics SK]]
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[[Category: Arp 2/3]]
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[[Category: Gautreau A]]
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[[Category: Arpin]]
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[[Category: Cell migration]]
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[[Category: Protein binding]]
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Current revision

Hybrid structural analysis of the Arp2/3 regulator Arpin identifies its acidic tail as a primary binding epitope

PDB ID 4z68

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