https://doi.org/10.1007/978-1-...
Part of book or chapter of book . 1991 . Peer-reviewed
Data sources: Crossref
Time Dependent Heterodimer Formation Leads to Inhibition of HIV Protease Activity
Authors: L M, Babé; C S, Craik;
pmid: 1812756
Time Dependent Heterodimer Formation Leads to Inhibition of HIV Protease Activity
Abstract
The protease encoded by the human immunodefiency virus (HIV) is a homodimer as determined by X-ray crystallographic (Navia et al., 1989, Wlodawer et al., 1989) and biochemical analysis (Meek et al., 1989). A four-stranded antiparallel s-sheet generated by interdigitating N-and C-termini of the monomers dominates the dimer interface. This s-sheet is partially stabilized by intersubunit backbone H-bonds of alternate amino acids from each of the four strands.
Related Organizations
- University of California, San Francisco United States
Keywords
HIV Protease, Protein Conformation, HIV-2, HIV-1, Aspartic Acid Endopeptidases, HIV Protease Inhibitors, Recombinant Proteins
HIV Protease, Protein Conformation, HIV-2, HIV-1, Aspartic Acid Endopeptidases, HIV Protease Inhibitors, Recombinant Proteins
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