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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.