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Table 2 Drug binding site residues

From: Molecular models of human P-glycoprotein in two different catalytic states

Pose 1 2 3 4 5 6 7 8
Colchicine Gln946 Gln946 Ile306 Ile306 Ile306 Ile306 Ile306 Leu339
  Tyr950 Tyr950 Phe335 Phe335 Phe335 Phe335 Phe335 Gln725
  Tyr953 Tyr953 Phe728 Phe728 Leu339 Phe728 Phe728 Phe728
  Phe957 Phe957    Phe728    Phe983
   Leu975       
RhodamineB Leu65 His61 Phe728 Ile306 Ile306 Ile306 Ala311 Gln725
  Ile340 Leu65 Tyr950 Phe335 Phe335 Phe728 Phe335 Phe728
  Phe343 Val125 Tyr953 Phe728 Phe728 Phe983 Phe728 Phe983
  Phe942 Phe938 Phe957 Phe983 Phe983    
  Tyr950   Leu975      
  Tyr953        
  Phe957        
  Val982        
Verapamil Ile306 Ile306 Ile306 Ala311 Leu65 Ile306 Ile306 Leu975
  Phe335 Leu339 Phe335 Phe335 Val125 Phe335 Phe335 Thr333
  Leu339 Phe343 Phe728 Phe728 Phe942 Leu339 Leu339  
  Gln725 Gln725   Leu975   Phe345   
  Phe728 Phe728       
  Val125 Ile306 Val125 Val125 Leu65 Ile306 Ile306 Phe343
  Ile340 Phe335 Leu339 Leu339 Ile340 Thr333 Phe335 Gln725
  Phe343 Leu339 Ile340 Ile340 Phe343 Phe335 Leu339 Phe728
Vinblastine Phe942 Ile340 Phe343 Phe343 Phe728 Leu339 Phe343 Ser766
  Gln946 Phe343 Phe938 Phe942 Gln946 Ile340 Phe728 Phe983
  Val982 Phe728 Phe942 Val982 Phe983 Phe728 Phe983  
  Phe983 Phe983 Phe983 Phe983   Phe983   
  1. Residues found to interact with each of the 8 predicted positions of the four different ligands (see text) docked in the central cavity of the closed nucleotide-free structure. The residues experimentally identified to alter the specificity of a particular ligand are reported in bold and underlined.