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==Structure of fragment of human end-binding protein 1 (EB1) containing the N-terminal domain at 1.35 A resolution==
==Structure of fragment of human end-binding protein 1 (EB1) containing the N-terminal domain at 1.35 A resolution==
<StructureSection load='2r8u' size='340' side='right' caption='[[2r8u]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
<StructureSection load='2r8u' size='340' side='right'caption='[[2r8u]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2r8u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R8U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R8U FirstGlance]. <br>
<table><tr><td colspan='2'>[[2r8u]] 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=2R8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R8U FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</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]] 1.35&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pa7|1pa7]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</scene></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=2r8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r8u OCA], [http://pdbe.org/2r8u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r8u RCSB], [http://www.ebi.ac.uk/pdbsum/2r8u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2r8u 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=2r8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r8u OCA], [https://pdbe.org/2r8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r8u RCSB], [https://www.ebi.ac.uk/pdbsum/2r8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r8u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MARE1_HUMAN MARE1_HUMAN]] 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. May play a role in cell migration.<ref>PMID:12388762</ref> <ref>PMID:21646404</ref> <ref>PMID:16109370</ref> <ref>PMID:19632184</ref>
[https://www.uniprot.org/uniprot/MARE1_HUMAN MARE1_HUMAN] 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. May play a role in cell migration.<ref>PMID:12388762</ref> <ref>PMID:21646404</ref> <ref>PMID:16109370</ref> <ref>PMID:19632184</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r8/2r8u_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r8/2r8u_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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=2r8u ConSurf].
</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=2r8u ConSurf].
<div style="clear:both"></div>
<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 ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Huang, X]]
[[Category: Large Structures]]
[[Category: Lebioda, L]]
[[Category: Huang X]]
[[Category: Lovelace, L L]]
[[Category: Lebioda L]]
[[Category: Smith, D]]
[[Category: Lovelace LL]]
[[Category: Acetylation]]
[[Category: Smith D]]
[[Category: Cell cycle]]
[[Category: Cell division]]
[[Category: Cytoplasm]]
[[Category: Cytoskeleton]]
[[Category: Microtubule]]
[[Category: Mitosis]]
[[Category: Phosphorylation]]

Latest revision as of 08:34, 13 August 2026

Structure of fragment of human end-binding protein 1 (EB1) containing the N-terminal domain at 1.35 A resolution

2r8u, resolution 1.35Å

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