1v5k
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1v5k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v5k" /> '''Solution structure of the CH domain from mou...) |
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| - | [[Image:1v5k.jpg|left|200px]]<br /><applet load="1v5k" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1v5k" /> | ||
| - | '''Solution structure of the CH domain from mouse EB-1'''<br /> | ||
| - | == | + | ==Solution structure of the CH domain from mouse EB-1== |
| - | + | <StructureSection load='1v5k' size='340' side='right'caption='[[1v5k]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | [[ | + | <table><tr><td colspan='2'>[[1v5k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V5K FirstGlance]. <br> |
| - | [ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1v5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v5k OCA], [https://pdbe.org/1v5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v5k RCSB], [https://www.ebi.ac.uk/pdbsum/1v5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v5k ProSAT], [https://www.topsan.org/Proteins/RSGI/1v5k TOPSAN]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | [ | + | [https://www.uniprot.org/uniprot/MARE1_MOUSE MARE1_MOUSE] Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement. Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules. Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (By similarity). May play a role in cell migration (PubMed:15311282).[UniProtKB:Q15691]<ref>PMID:15311282</ref> |
| - | + | == Evolutionary Conservation == | |
| - | [ | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | [ | + | Check<jmol> |
| - | [[ | + | <jmolCheckbox> |
| - | [ | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v5/1v5k_consurf.spt"</scriptWhenChecked> |
| - | [[ | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | [ | + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1v5k ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| + | *[[End-binding protein|End-binding protein]] | ||
| + | *[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Inoue M]] | ||
| + | [[Category: Kigawa T]] | ||
| + | [[Category: Koshiba S]] | ||
| + | [[Category: Tomizawa T]] | ||
| + | [[Category: Yokoyama S]] | ||
Current revision
Solution structure of the CH domain from mouse EB-1
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