3gjo

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[[Image:3gjo.png|left|200px]]
 
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==Crystal structure of human EB1 in complex with microtubule Tip localization signal peptide of MACF==
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The line below this paragraph, containing "STRUCTURE_3gjo", creates the "Structure Box" on the page.
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<StructureSection load='3gjo' size='340' side='right'caption='[[3gjo]], [[Resolution|resolution]] 2.50&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'>[[3gjo]] is a 8 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=3GJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GJO 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]] 2.5&#8491;</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=3gjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gjo OCA], [https://pdbe.org/3gjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gjo RCSB], [https://www.ebi.ac.uk/pdbsum/3gjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gjo ProSAT]</span></td></tr>
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{{STRUCTURE_3gjo| PDB=3gjo | SCENE= }}
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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/gj/3gjo_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=3gjo 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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Microtubules are filamentous polymers essential for cell viability. Microtubule plus-end tracking proteins (+TIPs) associate with growing microtubule plus ends and control microtubule dynamics and interactions with different cellular structures during cell division, migration, and morphogenesis. EB1 and its homologs are highly conserved proteins that play an important role in the targeting of +TIPs to microtubule ends, but the underlying molecular mechanism remains elusive. By using live cell experiments and in vitro reconstitution assays, we demonstrate that a short polypeptide motif, Ser-x-Ile-Pro (SxIP), is used by numerous +TIPs, including the tumor suppressor APC, the transmembrane protein STIM1, and the kinesin MCAK, for localization to microtubule tips in an EB1-dependent manner. Structural and biochemical data reveal the molecular basis of the EB1-SxIP interaction and explain its negative regulation by phosphorylation. Our findings establish a general "microtubule tip localization signal" (MtLS) and delineate a unifying mechanism for this subcellular protein targeting process.
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===Crystal structure of human EB1 in complex with microtubule Tip localization signal peptide of MACF===
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An EB1-binding motif acts as a microtubule tip localization signal.,Honnappa S, Gouveia SM, Weisbrich A, Damberger FF, Bhavesh NS, Jawhari H, Grigoriev I, van Rijssel FJ, Buey RM, Lawera A, Jelesarov I, Winkler FK, Wuthrich K, Akhmanova A, Steinmetz MO Cell. 2009 Jul 23;138(2):366-76. PMID:19632184<ref>PMID:19632184</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 3gjo" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19632184}}, 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 19632184 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_19632184}}
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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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[[3gjo]] is a 8 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=3GJO OCA].
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==Reference==
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<ref group="xtra">PMID:019632184</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Honnappa, S.]]
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[[Category: Large Structures]]
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[[Category: Steinmetz, M O.]]
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[[Category: Honnappa S]]
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[[Category: +tip protein complex]]
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[[Category: Steinmetz MO]]
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[[Category: Actin-binding]]
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[[Category: Actin-binding calcium]]
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[[Category: Apc/dynactin binding protein]]
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[[Category: Cell cycle]]
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[[Category: Cell division]]
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[[Category: Eb1 structural motif]]
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[[Category: Microtubule]]
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[[Category: Microtubule actin cross-linking factor]]
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[[Category: Mitosis]]
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[[Category: Phosphoprotein]]
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[[Category: Structural protein]]
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[[Category: Sxip motiff]]
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Current revision

Crystal structure of human EB1 in complex with microtubule Tip localization signal peptide of MACF

PDB ID 3gjo

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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