Structure-based analysis of HIV-1 protease-inhibitor binding

Structure—based analysis of HIV-1 protease-inhibitor binding 

The growing body of structural and thermodynamic data has revealed similarities and differences in molecular origins for inhibitors specificity against HIV-1 protease and its various mutant forms. The crystal structures of three 

Structure-based analysis of HIV-1 protease—SB203386 inhibitor binding 

A widely accepted two-step mechanism of HIV-1 protease binding implies the creation of a loose complex with the open form of the enzyme, followed by the conformational change involving the closure of the flap region over the active site and formation of the final bound complex. Consequently, binding affinity differences between the HIV-1 protease and its mutants may also result from the changes in the internal equilibrium between the bound form of the protease with closed flaps conformation and the unbound open form 

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II. Structure—based analysis of HIV-1 protease-inhibitor binding... 

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