2qjx

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(New page: 200px<br /><applet load="2qjx" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qjx, resolution 1.900&Aring;" /> '''Structural Basis of...)
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[[Image:2qjx.jpg|left|200px]]<br /><applet load="2qjx" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2qjx, resolution 1.900&Aring;" />
 
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'''Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1'''<br />
 
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==Overview==
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==Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1==
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Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus, ends of microtubules, where they stimulate microtubule growth and recruit, signaling molecules. Three main +TIP classes have been identified, (XMAP215, EB1, and CLIP-170), but whether they act upon microtubule plus, ends through a similar mechanism has not been resolved. Here, we report, crystal structures of the tubulin binding domains of XMAP215 (yeast Stu2p, and Drosophila Msps), EB1 (yeast Bim1p and human EB1), and CLIP-170, (human), which reveal diverse tubulin binding interfaces. Functional, studies, however, reveal a common property that native or artificial, dimerization of tubulin binding domains (including chemically induced, heterodimers of EB1 and CLIP-170) induces tubulin nucleation/assembly in, vitro and, in most cases, plus end tracking in living cells. We propose, that +TIPs, although diverse in structure, share a common property of, multimerizing tubulin, thus acting as polymerization chaperones that aid, in subunit addition to the microtubule plus end.
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<StructureSection load='2qjx' size='340' side='right'caption='[[2qjx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2qjx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QJX 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]] 1.9&#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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qjx OCA], [https://pdbe.org/2qjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qjx RCSB], [https://www.ebi.ac.uk/pdbsum/2qjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qjx ProSAT]</span></td></tr>
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</table>
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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/qj/2qjx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2qjx 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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Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170), but whether they act upon microtubule plus ends through a similar mechanism has not been resolved. Here, we report crystal structures of the tubulin binding domains of XMAP215 (yeast Stu2p and Drosophila Msps), EB1 (yeast Bim1p and human EB1), and CLIP-170 (human), which reveal diverse tubulin binding interfaces. Functional studies, however, reveal a common property that native or artificial dimerization of tubulin binding domains (including chemically induced heterodimers of EB1 and CLIP-170) induces tubulin nucleation/assembly in vitro and, in most cases, plus end tracking in living cells. We propose that +TIPs, although diverse in structure, share a common property of multimerizing tubulin, thus acting as polymerization chaperones that aid in subunit addition to the microtubule plus end.
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==About this Structure==
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Structural basis of microtubule plus end tracking by XMAP215, CLIP-170, and EB1.,Slep KC, Vale RD Mol Cell. 2007 Sep 21;27(6):976-91. PMID:17889670<ref>PMID:17889670</ref>
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2QJX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QJX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170, and EB1., Slep KC, Vale RD, Mol Cell. 2007 Sep 21;27(6):976-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17889670 17889670]
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</div>
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<div class="pdbe-citations 2qjx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Slep KC]]
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[[Category: Slep, K.C.]]
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[[Category: Vale RD]]
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[[Category: Vale, R.D.]]
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[[Category: calponin homology domain]]
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[[Category: protein binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:21:20 2008''
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Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1

PDB ID 2qjx

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