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Literature summary for 3.4.23.16 extracted from

  • Davis, D.A.; Tebbs, I.R.; Daniels, S.I.; Stahl, S.J.; Kaufman, J.D.; Wingfield, P.; Bowman, M.J.; Chmielewski, J.; Yarchoan, R.
    Analysis and characterization of dimerization inhibition of a multi-drug-resistant human immunodeficiency virus type 1 protease using a novel size-exclusion chromatographic approach (2009), Biochem. J., 419, 497-506.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
L10I/K45R/I54V/L63P/A71V/V82T/L90M/I93L dimerization study on mutant protease PRMDR derived from an HIV-1-infected patient on antiviral therapy. PRMDR contains eight drug-resistant related mutations that often arise in patients on antiviral therapy, none of these mutations reside in the N- or C-terminal regions that make up the dimerization interface. PRMDR is highly resistant to autoproteolysis. Incubation with dimerization inhibitors such as peptide P27 leads to dose- and time-dependent formation of protease monomers, while incubation with a active-site inhibitor does not change the elution profile of the protease. The monomeric protease induced by P27 has fluorescent characteristics consistent with unfolded protein Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
P27 peptide i.e. PQITLRKKRRQRRRPPQVSFNFCTLNF. Incubation of mutant L10I/K45R/I54V/L63P/A71V/V82T/L90M/I93L with peptide leads to dose- and time-dependent formation of protease monomers, while incubation with a active-site inhibitor does not change the elution profile of the protease. The monomeric protease induced by P27 has fluorescent characteristics consistent with unfolded protein Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
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