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Studies on flexibility and binding affinity of Asp25 of HIV-1 protease mutants.

International journal of biological macromolecules - 1 May 2008

Purohit Rituraj, Rajasekaran R, Sudandiradoss C, George Priya Doss C, Ramanathan K, Rao Sethumadhavan

Abstract excerpt

We have investigated and highlighted the behavior of binding residue, Asp25 by computational analysis, which play an important role in understanding docking process with drug molecule, Ritonavir (Norvir) and the flexibility nature of the Human Immunodeficiency Virus-1 (HIV-1) protease enzyme. It is well known that Ritonavir is a potent and a selective HIV-1 protease inhibitor. Molecular dockings were performed in...

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Aspartic Acid
HIV-1
HIV Protease
HIV Protease Inhibitors
Molecular Conformation

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Protein Conformation

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PMID: 18367244
DOI: 10.1016/j.ijbiomac.2008.01.011

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