6gze
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TBA1B_BOVIN TBA1B_BOVIN]] 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. [[http://www.uniprot.org/uniprot/STMN4_RAT STMN4_RAT]] Exhibits microtubule-destabilizing activity.<ref>PMID:15039434</ref> <ref>PMID:12111843</ref> <ref>PMID:15014504</ref> [[http://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] 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). | [[http://www.uniprot.org/uniprot/TBA1B_BOVIN TBA1B_BOVIN]] 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. [[http://www.uniprot.org/uniprot/STMN4_RAT STMN4_RAT]] Exhibits microtubule-destabilizing activity.<ref>PMID:15039434</ref> <ref>PMID:12111843</ref> <ref>PMID:15014504</ref> [[http://www.uniprot.org/uniprot/TBB2B_BOVIN TBB2B_BOVIN]] 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). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Microtubules (MTs) are hollow cylinders made of tubulin, a GTPase responsible for essential functions during cell growth and division, and thus, key target for anti-tumor drugs. In MTs, GTP hydrolysis triggers structural changes in the lattice, which are responsible for interaction with regulatory factors. The stabilizing GTP-cap is a hallmark of MTs and the mechanism of the chemical-structural link between the GTP hydrolysis site and the MT lattice is a matter of debate. We have analyzed the structure of tubulin and MTs assembled in the presence of fluoride salts that mimic the GTP-bound and GDP*Pi transition states. Our results challenge current models because tubulin does not change axial length upon GTP hydrolysis. Moreover, analysis of the structure of MTs assembled in the presence of several nucleotide analogues and of taxol allows us to propose that previously described lattice expansion could be a post-hydrolysis stage involved in Pi release. | ||
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| + | Structural model for differential cap maturation at growing microtubule ends.,Estevez-Gallego J, Josa-Prado F, Ku S, Buey RM, Balaguer FA, Prota AE, Lucena-Agell D, Kamma-Lorger C, Yagi T, Iwamoto H, Duchesne L, Barasoain I, Steinmetz MO, Chretien D, Kamimura S, Diaz JF, Oliva MA Elife. 2020 Mar 10;9. pii: 50155. doi: 10.7554/eLife.50155. PMID:32151315<ref>PMID:32151315</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6gze" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Stathmin-4 3D structures|Stathmin-4 3D structures]] | *[[Stathmin-4 3D structures|Stathmin-4 3D structures]] | ||
| + | *[[Tubulin 3D Structures|Tubulin 3D Structures]] | ||
| + | *[[Tubulin tyrosine ligase|Tubulin tyrosine ligase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Tubulin-GDP.BeF complex
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Categories: Bos taurus | Buffalo rat | Chick | Large Structures | Diaz, J F | Oliva, M A | Cell cycle | Cytoskeleton | Division | Gtpase
