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Medicine and Health Sciences

Selected Works

Celia A. Schiffer

Protein Structure, Tertiary

Articles 1 - 2 of 2

Full-Text Articles in Life Sciences

Crystal Structure Of Lysine Sulfonamide Inhibitor Reveals The Displacement Of The Conserved Flap Water Molecule In Human Immunodeficiency Virus Type 1 Protease, Madhavi Nalam, Anik Peeters, Tim Jonckers, Inge Dierynck, Celia Schiffer Nov 2011

Crystal Structure Of Lysine Sulfonamide Inhibitor Reveals The Displacement Of The Conserved Flap Water Molecule In Human Immunodeficiency Virus Type 1 Protease, Madhavi Nalam, Anik Peeters, Tim Jonckers, Inge Dierynck, Celia Schiffer

Celia A. Schiffer

Human immunodeficiency virus type 1 (HIV-1) protease has been continuously evolving and developing resistance to all of the protease inhibitors. This requires the development of new inhibitors that bind to the protease in a novel fashion. Most of the inhibitors that are on the market are peptidomimetics, where a conserved water molecule mediates hydrogen bonding interactions between the inhibitors and the flaps of the protease. Recently a new class of inhibitors, lysine sulfonamides, was developed to combat the resistant variants of HIV protease. Here we report the crystal structure of a lysine sulfonamide. This inhibitor binds to the active site …


Role Of Invariant Thr80 In Human Immunodeficiency Virus Type 1 Protease Structure, Function, And Viral Infectivity, Jennifer E. Foulkes-Murzycki, Moses Prabu-Jeyabalan, Deyna Cooper, Gavin J. Henderson, Janera Harris, Ronald I. Swanstrom, Celia A. Schiffer Nov 2011

Role Of Invariant Thr80 In Human Immunodeficiency Virus Type 1 Protease Structure, Function, And Viral Infectivity, Jennifer E. Foulkes-Murzycki, Moses Prabu-Jeyabalan, Deyna Cooper, Gavin J. Henderson, Janera Harris, Ronald I. Swanstrom, Celia A. Schiffer

Celia A. Schiffer

Sequence variability associated with human immunodeficiency virus type 1 (HIV-1) is useful for inferring structural and/or functional constraints at specific residues within the viral protease. Positions that are invariant even in the presence of drug selection define critically important residues for protease function. While the importance of conserved active-site residues is easily understood, the role of other invariant residues is not. This work focuses on invariant Thr80 at the apex of the P1 loop of HIV-1, HIV-2, and simian immunodeficiency virus protease. In a previous study, we postulated, on the basis of a molecular dynamics simulation of the unliganded protease, …