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    STUDIA CHEMIA - Issue no. 3 / 2011  
         
  Article:   X-RAY CRYSTAL STRUCTURE AND DYNAMICS REVEAL HIV-1 PROTEASE DRUG INTERACTIONS.

Authors:  YONG WANG, TAMARIA G. DEWDNEY, ZHIGANG LIU, SAMUEL J. REITER, JOSEPH S. BRUNZELLE, IULIA A. KOVARI, LADISLAU C. KOVARI. 		 
       
         
  Abstract:  The dynamic movement of HIV-1 protease is an important feature for inhibitor design. The wide-open form of multi-drug resistant HIV-1 protease solved by our group exhibits an increase in flap distance. Stabilizing the protease flaps could be a strategy to overcome drug resistance. A peptidic inhibitor stabilizing the protease-inhibitor complex and a structural novel inhibitor targeting the wide-open form protease have been identified as a new scaffold for drug development.

Keywords: multi-drug resistance, HIV-1 protease, drug design, 		 
         
     
         
         
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