3woy

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<StructureSection load='3woy' size='340' side='right'caption='[[3woy]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3woy' size='340' side='right'caption='[[3woy]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3woy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WOY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3woy]] 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=3WOY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WOY FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3woz|3woz]]</div></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]] 2.1&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLASP2, KIAA0627 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3woy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3woy OCA], [https://pdbe.org/3woy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3woy RCSB], [https://www.ebi.ac.uk/pdbsum/3woy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3woy ProSAT]</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=3woy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3woy OCA], [https://pdbe.org/3woy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3woy RCSB], [https://www.ebi.ac.uk/pdbsum/3woy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3woy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CLAP2_HUMAN CLAP2_HUMAN]] Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.<ref>PMID:11290329</ref> <ref>PMID:15631994</ref> <ref>PMID:16824950</ref> <ref>PMID:16866869</ref> <ref>PMID:16914514</ref> <ref>PMID:17543864</ref> <ref>PMID:20937854</ref>
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[https://www.uniprot.org/uniprot/CLAP2_HUMAN CLAP2_HUMAN] Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules. Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towards the leading edge of the cell. May act at the cell cortex to enhance the frequency of rescue of depolymerizing microtubules by attaching their plus-ends to cortical platforms composed of ERC1 and PHLDB2. This cortical microtubule stabilizing activity is regulated at least in part by phosphatidylinositol 3-kinase signaling. Also performs a similar stabilizing function at the kinetochore which is essential for the bipolar alignment of chromosomes on the mitotic spindle. Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex.<ref>PMID:11290329</ref> <ref>PMID:15631994</ref> <ref>PMID:16824950</ref> <ref>PMID:16866869</ref> <ref>PMID:16914514</ref> <ref>PMID:17543864</ref> <ref>PMID:20937854</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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CLIP-associated proteins CLASPs are mammalian microtubule (MT) plus-end tracking proteins (+TIPs) that promote MT rescue in vivo. Their plus-end localization is dependent on other +TIPs, EB1 and CLIP-170, but in the leading edge of the cell, CLASPs display lattice-binding activity. MT association of CLASPs is suggested to be regulated by multiple TOG (tumor overexpressed gene) domains and by the serine-arginine (SR)-rich region, which contains binding sites for EB1. Here, we report the crystal structures of the two TOG domains of CLASP2. Both domains consist of six HEAT repeats, which are similar to the canonical paddle-like tubulin-binding TOG domains, but have arched conformations. The degrees and directions of curvature are different between the two TOG domains, implying that they have distinct roles in MT binding. Using biochemical, molecular modeling and cell biological analyses, we have investigated the interactions between the TOG domains and alphabeta-tubulin and found that each domain associates differently with alphabeta-tubulin. Our findings suggest that, by varying the degrees of domain curvature, the TOG domains may distinguish the structural conformation of the tubulin dimer, discriminate between different states of MT dynamic instability and thereby function differentially as stabilizers of MTs.
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CLASP2 Has Two Distinct TOG Domains That Contribute Differently to Microtubule Dynamics.,Maki T, Grimaldi AD, Fuchigami S, Kaverina I, Hayashi I J Mol Biol. 2015 Jul 17;427(14):2379-95. doi: 10.1016/j.jmb.2015.05.012. Epub, 2015 May 21. PMID:26003921<ref>PMID:26003921</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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<div class="pdbe-citations 3woy" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hayashi, I]]
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[[Category: Hayashi I]]
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[[Category: Maki, T]]
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[[Category: Maki T]]
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[[Category: Heat repeat]]
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[[Category: Microtubule]]
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[[Category: Microtubule binding]]
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[[Category: Structural protein]]
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[[Category: Tubulin]]
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[[Category: Unknown]]
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Current revision

Crystal structure of CLASP2 TOG domain (TOG2)

PDB ID 3woy

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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