1yib

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(New page: 200px<br /> <applet load="1yib" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yib, resolution 1.80&Aring;" /> '''Crystal Structure o...)
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[[Image:1yib.gif|left|200px]]<br />
 
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<applet load="1yib" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yib, resolution 1.80&Aring;" />
 
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'''Crystal Structure of the Human EB1 C-terminal Dimerization Domain'''<br />
 
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==Overview==
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==Crystal Structure of the Human EB1 C-terminal Dimerization Domain==
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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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<StructureSection load='1yib' size='340' side='right'caption='[[1yib]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1yib]] 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=1YIB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YIB 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]] 1.8&#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=1yib FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yib OCA], [https://pdbe.org/1yib PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yib RCSB], [https://www.ebi.ac.uk/pdbsum/1yib PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yib 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/1yib_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=1yib ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1YIB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YIB OCA].
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*[[End-binding protein|End-binding protein]]
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*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
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==Reference==
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== References ==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15699215 15699215]
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<references/>
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__TOC__
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</StructureSection>
[[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: Elliott, S.L.]]
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[[Category: Elliott SL]]
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[[Category: Kolodziej, P.A.]]
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[[Category: Kolodziej PA]]
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[[Category: Ohkura, H.]]
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[[Category: Ohkura H]]
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[[Category: Rogers, S.L.]]
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[[Category: Rogers SL]]
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[[Category: Slep, K.C.]]
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[[Category: Slep KC]]
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[[Category: Vale, R.D.]]
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[[Category: Vale RD]]
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[[Category: coiled coil; four helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:20:19 2007''
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Current revision

Crystal Structure of the Human EB1 C-terminal Dimerization Domain

PDB ID 1yib

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