1yib
From Proteopedia
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==Crystal Structure of the Human EB1 C-terminal Dimerization Domain== | ==Crystal Structure of the Human EB1 C-terminal Dimerization Domain== | ||
- | <StructureSection load='1yib' size='340' side='right' caption='[[1yib]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='1yib' size='340' side='right'caption='[[1yib]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1yib]] is a 1 chain structure with sequence from [ | + | <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> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</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=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> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [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/yi/1yib_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yi/1yib_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/ | + | </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]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 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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- | 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> | ||
- | + | ==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: Elliott | + | [[Category: Large Structures]] |
- | [[Category: Kolodziej | + | [[Category: Elliott SL]] |
- | [[Category: Ohkura | + | [[Category: Kolodziej PA]] |
- | [[Category: Rogers | + | [[Category: Ohkura H]] |
- | [[Category: Slep | + | [[Category: Rogers SL]] |
- | [[Category: Vale | + | [[Category: Slep KC]] |
- | + | [[Category: Vale RD]] | |
- | + | ||
- | + |
Current revision
Crystal Structure of the Human EB1 C-terminal Dimerization Domain
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Categories: Homo sapiens | Large Structures | Elliott SL | Kolodziej PA | Ohkura H | Rogers SL | Slep KC | Vale RD