Issue 15, 2004
From the journal:

Organic & Biomolecular Chemistry

Microtubule structure and its stabilisation

Linda A. Amos*a  

* Corresponding authors

a MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK
E-mail: laa@mrc-lmb.cam.ac.uk

Abstract

Microtubules are designed to be dynamically unstable. GTP hydrolysis converts an initially stable polymeric structure into an unstable one in which strain at the interfaces between longitudinal neighbours in the helical lattice of subunits is balanced by lateral interactions. However, stability can be modulated by a variety of factors, including associated proteins and a variety of drug molecules. Stabilising drugs such as Taxol and the assembly-promoting repeat motifs of tau protein occupy a special pocket in β-tubulin. Microtubule destabilising drugs such as colchicine alter the longitudinal interfaces of the subunits so that they cannot assemble into a microtubule lattice. These mechanisms are discussed in terms of the atomic structure of the protein.

Graphical abstract: Microtubule structure and its stabilisation

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Article information

DOI
https://doi.org/10.1039/B403634D
Article type
Perspective
Submitted
10 Mar 2004
Accepted
21 May 2004
First published
14 Jul 2004

Org. Biomol. Chem., 2004,2, 2153-2160

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Microtubule structure and its stabilisation

L. A. Amos, Org. Biomol. Chem., 2004, 2, 2153 DOI: 10.1039/B403634D

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