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Multiple sequence analysis of tubulin 1SA0 and human β-tubulin isotypes.

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posted on 2016-05-26, 20:39 authored by Bajarang Vasant Kumbhar, Anubhaw Borogaon, Dulal Panda, Ambarish Kunwar

The isotype β_III shows change of Ala315 to Thr, Cys239 to Ser, and Thr351-to Val, Isotype β_II change of Val316 to Ile at the colchicine binding pocket. Region of changed residues at colchicine binding pocket are shown in red color.

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Exploring the Origin of Differential Binding Affinities of Human Tubulin Isotypes αβII, αβIII and αβIV for DAMA-Colchicine Using Homology Modelling, Molecular Docking and Molecular Dynamics Simulations

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Keywords

binding affinities Tubulin isotypes αβ II sequence analysis study tubulin isotypes show MM-GBSA binding free-energy calculation dynamics simulations results show colchicine binding pocket Differential Binding Affinities binding affinity dynamics simulation analysis residue variations DAMA-colchicine III IV Molecular Dynamics Simulations Tubulin isotypes binding free-energy

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