1v5k: Difference between revisions

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New page: 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 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 />


==About this Structure==
==Solution structure of the CH domain from mouse EB-1==
1V5K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V5K OCA].  
<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: Mus musculus]]
[[Category: Single protein]]
[[Category: Inoue M]]
[[Category: Inoue, M.]]
[[Category: Kigawa T]]
[[Category: Kigawa, T.]]
[[Category: Koshiba S]]
[[Category: Koshiba, S.]]
[[Category: Tomizawa T]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[Category: Yokoyama S]]
[[Category: Tomizawa, T.]]
[[Category: Yokoyama, S.]]
[[Category: adenomatosis polyposis coli binding protein]]
[[Category: calponin homology (ch) domain]]
[[Category: microtubule binding]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: structural genomics]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:26:59 2007''

Latest revision as of 02:57, 28 December 2023

Solution structure of the CH domain from mouse EB-1Solution structure of the CH domain from mouse EB-1

Structural highlights

1v5k is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

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][1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Wen Y, Eng CH, Schmoranzer J, Cabrera-Poch N, Morris EJ, Chen M, Wallar BJ, Alberts AS, Gundersen GG. EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration. Nat Cell Biol. 2004 Sep;6(9):820-30. Epub 2004 Aug 15. PMID:15311282 doi:http://dx.doi.org/10.1038/ncb1160
Drag the structure with the mouse to rotate

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