1ueg

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{{Seed}}
 
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[[Image:1ueg.png|left|200px]]
 
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==Crystal structure of amino-terminal microtubule binding domain of EB1==
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The line below this paragraph, containing "STRUCTURE_1ueg", creates the "Structure Box" on the page.
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<StructureSection load='1ueg' size='340' side='right'caption='[[1ueg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ueg]] 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=1UEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UEG FirstGlance]. <br>
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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]] 2.4&#8491;</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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{{STRUCTURE_1ueg| PDB=1ueg | SCENE= }}
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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=1ueg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ueg OCA], [https://pdbe.org/1ueg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ueg RCSB], [https://www.ebi.ac.uk/pdbsum/1ueg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ueg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ue/1ueg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ueg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The end-binding protein 1 (EB1) family is a highly conserved group of proteins that localizes to the plus-ends of microtubules. EB1 has been shown to play an important role in regulating microtubule dynamics and chromosome segregation, but its regulation mechanism is poorly understood. We have determined the 1.45-A resolution crystal structure of the amino-terminal domain of EB1, which is essential for microtubule binding, and show that it forms a calponin homology (CH) domain fold that is found in many proteins involved in the actin cytoskeleton. The functional CH domain for actin binding is a tandem pair, whereas EB1 is the first example of a single CH domain that can associate with the microtubule filament. Although our biochemical study shows that microtubule binding of EB1 is electrostatic in part, our mutational analysis suggests that the hydrophobic network, which is partially exposed in our crystal structure, is also important for the association. We propose that, like other actin-binding CH domains, EB1 employs the hydrophobic interaction to bind to microtubules.
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===Crystal structure of amino-terminal microtubule binding domain of EB1===
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Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1).,Hayashi I, Ikura M J Biol Chem. 2003 Sep 19;278(38):36430-4. Epub 2003 Jul 11. PMID:12857735<ref>PMID:12857735</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 1ueg" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12857735}}, adds the Publication Abstract to the page
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*[[End-binding protein|End-binding protein]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12857735 is the PubMed ID number.
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*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_12857735}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1UEG is a [[Single protein]] structure of 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=1UEG OCA].
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==Reference==
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Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)., Hayashi I, Ikura M, J Biol Chem. 2003 Sep 19;278(38):36430-4. Epub 2003 Jul 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12857735 12857735]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hayashi, I.]]
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[[Category: Hayashi I]]
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[[Category: Ikura, M.]]
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[[Category: Ikura M]]
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[[Category: Ch domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:25:58 2008''
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Current revision

Crystal structure of amino-terminal microtubule binding domain of EB1

PDB ID 1ueg

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