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Table 2 Residue changes between β-tubulin isotypes in the binding site for peloruside A and laulimalide

From: Determination of the optimal tubulin isotype target as a method for the development of individualized cancer chemotherapy

Isotype

Residue changes in the peloruside/laulimalide binding site

βIIa

C200S

V292M

A295S

   

βIIb

 

V292M

A295S

   

βIII

 

V292M

    

βIVa

 

V292M

    

βIVb

 

V292M

    

βV

 

V292M

K296R

   

βVI

 

V292M

K296R

M298T

  

Isotype

Residue changes in the peloruside/laulimalide binding site

βIII

    

N331A

V332I

βIVa

    

N331S

 

βV

    

N331A

V332I

βVI

P304L

H306R

M329L

 

N331S

 

Isotype

Residue changes in the peloruside/laulimalide binding site

βIII

N334S

     

βIVa

N334S

     

βV

N334S

     

βVI

N334T

K335R

Y339C

   
  1. Residue changes between β-tubulin isotypes with respect to the interactions with two novel spindle poisons, peloruside A and laulimalide, divided into three distinct regions that contribute to the interactions between the protein and the ligands.