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2qjx
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2qjx" size="350" color="white" frame="true" align="right" spinBox="true" caption="2qjx, resolution 1.900Å" /> '''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" | ||
| - | caption="2qjx, resolution 1.900Å" /> | ||
| - | '''Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1'''<br /> | ||
| - | == | + | ==Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1== |
| - | Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus | + | <StructureSection load='2qjx' size='340' side='right'caption='[[2qjx]], [[Resolution|resolution]] 1.90Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2qjx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qjz|2qjz]], [[2qk0|2qk0]], [[2qk1|2qk1]], [[2qk2|2qk2]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BIM1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/BIM1_YEAST BIM1_YEAST]] Binds microtubules. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qj/2qjx_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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/main_output.php?pdb_ID=2qjx ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2qjx" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Slep, K | + | <references/> |
| - | [[Category: Vale, R | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Atcc 18824]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Slep, K C]] | |
| + | [[Category: Vale, R D]] | ||
| + | [[Category: Calponin homology domain]] | ||
| + | [[Category: Protein binding]] | ||
Current revision
Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1
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