1yig

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{{Seed}}
 
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[[Image:1yig.png|left|200px]]
 
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==Crystal Structure of the Human EB1 C-terminal Dimerization Domain==
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The line below this paragraph, containing "STRUCTURE_1yig", creates the "Structure Box" on the page.
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<StructureSection load='1yig' size='340' side='right'caption='[[1yig]], [[Resolution|resolution]] 2.00&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'>[[1yig]] 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=1YIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YIG 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&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1yig| PDB=1yig | 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=1yig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yig OCA], [https://pdbe.org/1yig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yig RCSB], [https://www.ebi.ac.uk/pdbsum/1yig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yig 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/yi/1yig_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=1yig 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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EB1 is a member of a conserved protein family that localizes to growing microtubule plus ends. EB1 proteins also recruit cell polarity and signaling molecules to microtubule tips. However, the mechanism by which EB1 recognizes cargo is unknown. Here, we have defined a repeat sequence in adenomatous polyposis coli (APC) that binds to EB1's COOH-terminal domain and identified a similar sequence in members of the microtubule actin cross-linking factor (MACF) family of spectraplakins. We show that MACFs directly bind EB1 and exhibit EB1-dependent plus end tracking in vivo. To understand how EB1 recognizes APC and MACFs, we solved the crystal structure of the EB1 COOH-terminal domain. The structure reveals a novel homodimeric fold comprised of a coiled coil and four-helix bundle motif. Mutational analysis reveals that the cargo binding site for MACFs maps to a cluster of conserved residues at the junction between the coiled coil and four-helix bundle. These results provide a structural understanding of how EB1 binds two regulators of microtubule-based cell polarity.
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===Crystal Structure of the Human EB1 C-terminal Dimerization Domain===
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Structural determinants for EB1-mediated recruitment of APC and spectraplakins to the microtubule plus end.,Slep KC, Rogers SL, Elliott SL, Ohkura H, Kolodziej PA, Vale RD J Cell Biol. 2005 Feb 14;168(4):587-98. Epub 2005 Feb 7. PMID:15699215<ref>PMID:15699215</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 1yig" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15699215}}, 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 15699215 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_15699215}}
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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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1YIG is a 2 chains structure of sequences 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=1YIG OCA].
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==Reference==
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<ref group="xtra">PMID:15699215</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Elliott, S L.]]
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[[Category: Large Structures]]
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[[Category: Kolodziej, P A.]]
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[[Category: Elliott SL]]
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[[Category: Ohkura, H.]]
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[[Category: Kolodziej PA]]
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[[Category: Rogers, S L.]]
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[[Category: Ohkura H]]
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[[Category: Slep, K C.]]
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[[Category: Rogers SL]]
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[[Category: Vale, R D.]]
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[[Category: Slep KC]]
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[[Category: Coiled coil]]
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[[Category: Vale RD]]
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[[Category: Four helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:49:51 2009''
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Current revision

Crystal Structure of the Human EB1 C-terminal Dimerization Domain

PDB ID 1yig

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