X-Ray Structure of HIV-1 Protease Tethered Dimer Complexed to Ritonavir

Authors: Amit Das,; Dharmaraj Ramachandra Rao,; Madhusoodan Vijayacharya Hosur,

Source: Protein and Peptide Letters, Volume 14, Number 6, June 2007 , pp. 565-568(4)

Publisher: Bentham Science Publishers

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Abstract:

We report here the 2.5Å structure of HIV-1 protease tethered-dimer ritonavir complex. The inhibitor bound in the active site has different conformations in the two orientations. There is only one hydrogen bond between the inhibitor and the enzyme. The conserved flap-water is not found in the present complex.

Keywords: HIV-1 protease; tethered dimmer; inhibitor; X-ray crystallography

Document Type: Research article

Publication date: 2007-06-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.