6gwc: Difference between revisions

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'''Unreleased structure'''


The entry 6gwc is ON HOLD  until Paper Publication
==Tubulin:iE5 alphaRep complex==
<StructureSection load='6gwc' size='340' side='right' caption='[[6gwc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gwc]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GWC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GWC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gwc OCA], [http://pdbe.org/6gwc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gwc RCSB], [http://www.ebi.ac.uk/pdbsum/6gwc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gwc ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/D0VWY9_SHEEP D0VWY9_SHEEP]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).[RuleBase:RU003505]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microtubules are cytoskeletal filaments of eukaryotic cells made of alphabeta-tubulin heterodimers. Structural studies of non-microtubular tubulin rely mainly on molecules that prevent its self-assembly and are used as crystallization chaperones. Here we identified artificial proteins from an alphaRep library that are specific to alpha-tubulin. Turbidity experiments indicate that these alphaReps impede microtubule assembly in a dose-dependent manner and total internal reflection fluorescence microscopy further shows that they specifically block growth at the microtubule (-) end. Structural data indicate that they do so by targeting the alpha-tubulin longitudinal surface. Interestingly, in one of the complexes studied, the alpha subunit is in a conformation that is intermediate between the ones most commonly observed in X-ray structures of tubulin and those seen in the microtubule, emphasizing the plasticity of tubulin. These alpha-tubulin-specific alphaReps broaden the range of tools available for the mechanistic study of microtubule dynamics and its regulation.


Authors:  
Selection and Characterization of Artificial Proteins Targeting the Tubulin alpha Subunit.,Campanacci V, Urvoas A, Consolati T, Cantos-Fernandes S, Aumont-Nicaise M, Valerio-Lepiniec M, Surrey T, Minard P, Gigant B Structure. 2018 Dec 17. pii: S0969-2126(18)30457-X. doi:, 10.1016/j.str.2018.12.001. PMID:30661854<ref>PMID:30661854</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6gwc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ovis aries]]
[[Category: Campanacci, V]]
[[Category: Gigant, B]]
[[Category: Alpharep]]
[[Category: Artificial protein]]
[[Category: Cell cycle]]
[[Category: Cytoskeleton]]
[[Category: Microtubule]]

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