Structural Comparison of the Interaction of Tubulin with Various Ligands Affecting Microtubule Dynamics

Author(s): E. Stec-Martyna, M. Ponassi, M. Miele, S. Parodi, L. Felli, C. Rosano.

Journal Name: Current Cancer Drug Targets

Volume 12 , Issue 6 , 2012

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Microtubules (MTs), which are highly dynamic assemblies of the protein tubulin, play important and diverse roles in eukaryotic cells. MT dynamics are regulated during the cell cycle by interacting with a large number of endogenous cellular regulators. In addition, many anti-tumour drugs and natural ligands that interact directly with tubulin are able to either stabilise or destabilise MTs and to disrupt the normal dynamics. Herein, we compare the structures of tubulin when complexed with different ligands in order to analyse: (i) various binding-sites of the protein and different positions of ligands within the microtubule (ii) the diverse effect on the microtubule dynamics. The structures and data given are essential for understanding tubulin-ligand interactions and their influence on the regulation of the microtubule system.

Keywords: Microtubules, microtubule-stabilising agent, structure based drug design, structure-activity relationship, tubulin, plus-end tracking proteins, Guanosine-5'-triphosphate, microtubule-associated proteins, microtubule-stabilising agent, microtubules, structure-activity relationship, stathmine-like domain, The tight complex tubulin/RB3-SLD

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Article Details

Year: 2012
Page: [658 - 666]
Pages: 9
DOI: 10.2174/156800912801784893
Price: $65

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